Prof Robert Huber
My interests centre on the understanding of the structure and function of biological macromolecules. My work has included studies on proteases and their natural and synthetic inhibitors, metalloenzymes (iron, nickel, molybdenum, copper), proteins of the immune system (antibodies and antibody receptors), protein hormones and their receptors, protein kinases, enzymes of amino acid biosynthesis, enzymes of cofactor and vitamin biosynthesis and proteins of energy and electron transfer. In addition, I am interested in the development of instrumentation for data collection and of methods in protein crystallography, ranging from Patterson methods, graphic methods, and refinement, to the use of electron rich metal clusters, and most recently to the methods and instruments for crystal improvement.
Velarde, M., Huber, R., Yanagisawa, S., Dennison, C. and Messerschmidt, A. (2007) Influence of loop shortening on the metal binding site of Cupredoxin Pseudoazurin. Biochemistry 46, 9981-9991.
Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., Zanda, M., Bode, W. and Goettig, P. (2007) Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible Arg424 side-chain to selectivity. J. Mol. Biol. 371, 989-1006.
Borelli, C., Ruge, E., Schaller, M., Monod, M., Korting, H. C., Huber, R. and Maskos, K. (2007) The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A. Proteins 68, 738-748.
Kyrieleis, O. J., Huber, R., Ong, E., Oehler, R., Hunter, M., Madison, E. L. and Jacob, U. (2007) Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family. FEBS J. 274, 2148-2160.
Steiner, T., Lamerz, A. C., Hess, P., Breithaupt, C., Krapp, S., Bourenkov, G., Huber, R., Gerardy-Schahn, R. and Jacob, U. (2007) Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major. J. Biol. Chem. 282, 13003-13010.
Keil, C., Maskos, K., Than, M., Hoopes, J. T., Huber, R., Tan, F., Deddish, P. A., Erdos, E. G., Skidgel, R. A. and Bode, W. (2007) Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. J. Mol. Biol. 366, 504-516.
Breithaupt, C., Kurzbauer, R., Lilie, H., Schaller, A., Strassner, J., Huber, R., Macheroux, P. and Clausen, T. (2006) Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization. Proc. Natl. Acad. Sci. USA 103, 14337-14342.
Tamulaitiene, G., Jakubauskas, A., Urbanke, C., Huber, R., Grazulis, S. and Siksnys, V. (2006) The crystal structure of the rare-cutting restriction enzyme SdaI reveals unexpected domain architecture. Structure 14, 1389-1400.
Debela, M., Magdolen, V., Grimminger, V., Sommerhoff, C., Messerschmidt, A., Huber, R., Friedrich, R., Bode, W. and Goettig, P. (2006) Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. J. Mol. Biol. 362, 1094-1107.
Sitar, T., Popowicz, G. M., Siwanowicz, I., Huber, R. and Holak, T. A. (2006) Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins. Proc. Natl. Acad. Sci. USA 103, 13028-13033.
Kaiser, M., Groll, M., Siciliano, C., Götz, M., Assfalg-Machleidt, I., Kohno, J., Milbradt, A., Renner, C., Huber, R. and Moroder, L. (2005) Inhibition of yeast 20S proteasome by biaryl- ansbiaryl ether-cross-bridges tripeptide derivatives as TMC-95A analogs. Peptides, Biology and Chemistry. K. L. Liu and J. P. Tam. Monmouth Junction, Science Press USA Inc.
Chatwell, L., Krojer, T., Fidler, A., Römisch, W., Eisenreich, W., Bacher, A., Huber, R. and Fischer, M. (2006) Biosynthesis of riboflavin: Structure and properties of 2,5-Diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase of Methanocaldococcus jannaschii. J. Mol. Biol. 359, 1334-1351.
Groll, M., Huber, R. and Potts, B. C. (2006) Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of b-lactone ring opening and a mechanism for irreversible binding. J. Am. Chem. Soc. 128, 5136-5141.
Groll, M., Larionov, O. V., Huber, R. and de Meijere, A. (2006) Inhibitor-binding mode of homobelactosin C to proteasomes: New insights into class I MHC ligand generation. Proc. Natl. Acad. Sci. USA 103, 4576-4579.
Einsle, O., Niessen, H., Abt, D. J., Seiffert, G., Schink, B., Huber, R., Messerschmidt, A. and Kroneck, P. M. (2005) Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus. Acta Cryst. F61, 299-301.
Rohr, K. B., Selwood, T., Marquardt, U., Huber, R., Schechter, N. M., Bode, W. and Than, M. E. (2005) X-ray structures of free and leupeptin-complexed human aI-tryptase mutants: Indication for an a-->b-tryptase transition. J. Mol. Biol. 357, 195-209.
Kaiser, M., Groll, M., Götz, M., Siciliano, C., Assfalg-Machleidt, I., Weyher, E., Kohno, J., Milbradt, A., Renner, C., Huber, R. and Moroder, L. (2005) Structural determinants for 20S proteasome inhibition by TMC-95A. Peptides 2004. M. Flegel, M. Fridkin, C. Gilon and J. Slaninova. Geneve, Kenes International: 657-658.
Engel, M., Hoffmann, T., Manhart, S., Heiser, U., Chambre, S., Huber, R., Demuth, H. U. and Bode, W. (2006) Rigidity and flexibility of Dipeptidyl Peptidase IV: Crystal structures of and docking experiments with DPIV. J. Mol. Biol. 355, 768-783.
Golbik, R., Yu, C., Weyher-Stingl, E., Huber, R., Moroder, L., Budisa, N. and Schiene-Fischer, C. (2005) Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates. Biochemistry 44, 16026-16034.
Ramsperger, A., Augustin, M., Schott, A. K., Gerhardt, S., Krojer, T., Eisenreich, W., Illarionov, B., Cushman, M., Bacher, A., Huber, R. and Fischer, M. (2006) Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: Stereochemical implications. J. Biol. Chem. 281, 1224-1232.
Grazulis, S., Manakova, E., Roessle, M., Bochtler, M., Tamulaitiene, G., Huber, R. and Siksnys, V. (2005) Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease. Proc. Natl. Acad. Sci. USA 102, 15797-15802.
Breitenlechner, C. B., Kairies, N. A., Honold, K., Scheiblich, S., Koll, H., Greiter, E., Koch, S., Schafer, W., Huber, R. and Engh, R. A. (2005) Crystal structures of active Src kinase domain complexes. J. Mol. Biol. 353, 222-231.
Groll, M. and Huber, R. (2005) Purification, crystallization, and x-ray analysis of the yeast 20S proteasome. Methods in Enzymology 398, 329-336.
Arolas, J. L., Popowicz, G. M., Bronsoms, S., Aviles, F. X., Huber, R., Holak, T. A. and Ventura, S. (2005) Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: Contribution of the fourth disulfide bond. J. Mol. Biol. 352, 961-975.
Göttig, P. W., Brandstetter, H., Groll, M., Göhring, W., Konarev, P. V., Svergun, D. I., Huber, R. and Kim, J. S. (2005) X-ray snapshots of peptide processing in mutants of tricorn interacting factor F1 thermoplasma acidophilum. J. Biol. Chem. 280, 33387-33396.
Arolas, J. L., Popowicz, G. M., Lorenzo, J., Sommerhoff, C. P., Huber, R., Aviles, F. X. and Holak, T. A. (2005) The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode. J. Mol. Biol. 350, 489-498.
Kyrieleis, O. J., Göttig, P., Kiefersauer, R., Huber, R. and Brandstetter, H. (2005) Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations. J. Mol. Biol. 349, 787-800.
Than, M. E., Henrich, S., Bourenkov, G. P., Bartunik, H. D., Huber, R. and Bode, W. (2005) The endoproteinase furin contains two essential Ca 2+ ions stabilizing its N-terminus and the unique S1 specificity pocket. Acta Cryst. D61, 505-512.
Wisniewska, M., Bossenmaier, B., Georges, G., Hesse, F., Dangl, M., Kunkele, K. P., Ioannidis, I., Huber, R. and Engh, R. A. (2005) The 1.1Å resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity. J. Mol. Biol. 347, 1005-1014.
Bochtler, M., Groll, M., Brandstetter, H., Clausen, T. and Huber, R. (2005) Molecular machines for protein degradation. Protein Degradation. R. J. Mayer, A. Ciechanover and M. Rechsteiner. Weinheim, Wiley-VCH Verlag. 1: 248-287.
Fuentes-Prior, P. and Salvesen, G. S. (2004) The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384, 201-232.
Pal, P. P., Bae, J. H., Azim, M. K., Hess, P., Friedrich, R., Huber, R., Moroder, L. and Budisa, N. (2005) Structural and spectral response of Aequorea victoria green fluorescent proteins to chromophore fluorination. Biochemistry 44, 3663-3672.
Jauch, R., Humm, A., Huber, R. and Wahl, M. C. (2005) Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements. J. Biol. Chem. 280, 15131-15140.
Groll, M., Bochtler, M., Brandstetter, H., Clausen, T. and Huber, R. (2005) Molecular machines for protein degradation. CHEMBIOCHEM 6, 222-256.
Theodoratou, E., Huber, R. and Böck, A. (2005) [NiFe]-Hydrogenase maturation endopeptidase: structure and function. Biochem. Soc. Trans. 33, 108-111.
Siwanowicz, I., Popowicz, G. M., Wisniewska, M., Huber, R., Künkele, K. P., Lang, K., Engh, R. A. and Holak, T. A. (2005) Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure 13, 155-167.
Breitenlechner, C. B., Friebe, W. G., Brunet, E., Werner, G., Graul, K., Thomas, U., Künkele, K. P., Schäfer, W., Gassel, M., Bossemeyer, D., Huber, R., Engh, R. A. and Masjost, B. (2005) Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants. J. Med. Chem. 48, 163-170.
Wenig, K., Chatwell, L., von Pawel-Rammingen, U., Bjorck, L., Huber, R. and Sondermann, P. (2004) Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. Proc. Natl. Acad. Sci. USA 101, 17371-17376.
Groll, M. and Huber, R. (2004) Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach. Biochim. Biophys. Acta 1695, 33-44.
Paschos, A., Theodoratou, E., Fritsche, E., Böck, A. and Huber, R. (2004) Hydrogenase maturation endopeptidase. Handbook of Proteolytic Enzymes 2nd Edn, Elsevier Ltd.: 980-982.
Stanitzek, S., Augustin, M. A., Huber, R., Kupke, T. and Steinbacher, S. (2004) Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase. Structure 12, 1977-1988.
Kaiser, M., Milbradt, A. G., Renner, C., Assfalg-Machleidt, I., Groll, M., Huber, R. and Moroder, L. (2004) Cyclic Biphenyl Ether Tripeptides as Proteasome Inhibitors. Peptides. Peptide Revolution: Genomics, Proteomics & Therapeutics. M. Chorev and T. K. Sawyer. Cardiff, USA, American Chemical Society: 348-349.
Fischer, M., Schott, A. K., Römisch, W., Ramsperger, A., Augustin, M., Fidler, A., Bacher, A., Richter, G., Huber, R. and Eisenreich, W. (2004) Evolution of vitamin B2 biosynthesis. A novel class of riboflavin synthase in Archaea. J. Mol. Biol.343, 267-278.
Bonin, I., Mühlberger, R., Bourenkov, G. P., Huber, R., Bacher, A., Richter, G. and Wahl, M. C. (2004) Structural basis for the interaction of Escherichia coli NusA with protein N of phage l. Proc. Natl. Acad. Sci. USA 101, 13762-13767.
Popowicz, G. M., Müller, R., Noegel, A. A., Schleicher, M., Huber, R. and Holak, T. A. (2004) Molecular structure of the rod domain of Dictyostelium filamin. J. Mol. Biol. 342, 1637-1646.
Groll, M. and Huber, R. (2004) Structures of the Yeast Proteasome Core Particle in Complex with Inhibitors. Cancer Drug Discovery and Development: Proteasome Inhibitors in Cancer Therapy. J. Adams. Totowa, NJ, Humana Press Inc.: 39-46.
Keil, C., Huber, R., Bode, W. and Than, M. E. (2004) Cloning, expression, crystallization and initial crystallographic analysis of the C-terminal domain of the amyloid precursor protein APP. Acta Cryst. D60, 1614-1617.
Echt, S., Bauer, S., Steinbacher, S., Huber, R., Bacher, A. and Fischer , M. (2004) Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans. J. Mol. Biol. 341, 1085-1096.
Bonin, I., Martins, B. M., Purvanov, V., Fetzner, S., Huber, R. and Dobbek, H. (2004) Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase. Structure 12, 1425-1435.
Koch, M., Breithaupt, C., Gerhardt, S., Haase, I., Weber, S., Cushman, M., Huber, R., Bacher, A. and Fischer, M. (2004) Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase. Eur. J. Biochem. 271, 3208-3214.
Laupitz, R., Hecht, S., Amslinger, S., Zepeck, F., Kaiser, J., Richter, G., Schramek, N., Steinbacher, S., Huber, R., Arigoni, D., Bacher, A., Eisenreich, W. and Rohdich, F. (2004) Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways. Eur. J. Biochem. 271, 2658-2669.
Breitenlechner, C., Engh, R. A., Huber, R., Kinzel, V., Bossemeyer, D. and Gassel, M. (2004) The typically disordered N-Terminus of PKA can fold as a helix and project the myristoylation site into solution. Biochemistry 43, 7743-7749.
Bauer, S., Schott, A. K., Illarionova, V., Bacher, A., Huber, R. and Fischer, M. (2004) Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class. J. Mol. Biol. 339, 967-979.
Bader, G., Gomez-Ortiz, M., Haussmann, C., Bacher, A., Huber, R. and Fischer, M. (2004) Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli. Acta Cryst. D60, 1068-1075.
Fritze, I. M., Linden, L., Freigang, J., Auerbach, G., Huber, R. and Steinbacher, S. (2004) The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase. Plant Physiol. 134, 1388-1400.
Koch, M., Breithaupt, C., Kiefersauer, R., Freigang, J., Huber, R. and Messerschmidt, A. (2004) Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. EMBO J. 23, 1720-1728.
Breitenlechner, C. B., Wegge, T., Berillon, L., Graul, K., Marzenell, K., Friebe, W. G., Thomas, U., Schumacher, R., Huber, R., Engh, R. A. and Masjost, B. (2004) Structure-based optimization of novel Azepane derivatives as PKB inhibitors. J. Med. Chem. 47, 1375-1390.
Gaßel, M., Breitenlechner, C. B., König, N., Huber, R., Engh, R. A. and Bossemeyer, D. (2004) The protein kinase C inhibitor bisindolyl-maleimide II binds with reversed orientations to different conformations of PKA. J. Biol. Chem. 279, 23679-23690.
Than, M. E., Helm, M., Simpson, D. J., Lottspeich, F., Huber, R. and Gietl, C. (2004) The 2.0 Å crystal structure and substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm. J. Mol. Biol. 336, 1103-1116.
Svetlitchnyi, V., Dobbek, H., Meyer-Klaucke, W., Meins, T., Thiele, B., Römer, P., Huber, R. and Meyer, O. (2004) A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans. Proc. Natl. Acad. Sci. USA 101, 446-451.
Kim, J. S., Kluskens, L. D., de Vos, W. M., Huber, R. and van der Oost, J. (2004) Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin. J. Mol. Biol. 335, 787-797.
Breitenlechner, C., Gaßel, M., Hidaka, H., Kinzel, V., Huber, R., Engh, R. A. and Bossemeyer, D. (2003) Protein kinase A in complex with rho-kinase inhibitors Y-27632, fasudil, and H-1152P. Structural basis of selectivity. Structure 11, 1595-1607.
Hofmann, A. and Huber, R. (2003) Liposomes in assessment of annexin-membrane interactions. Methods in Enzymology, Liposomes. N. Duzgunes. New York, Academic Press. 372: 186-216.
Krapp, S., Münster-Kühnel, A. K., Kaiser, J. T., Huber, R., Tiralongo, J., Gerardy-Schahn, R. and Jacob, U. (2003) The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase. J. Mol. Biol. 334, 625-637.
Friedrich, R., Panizzi, P., Fuentes-Prior, P., Richter, K., Verhamme, I., Anderson, P. J., Kawabata, S., Huber, R., Bode, W. and Bock, P. E. (2003) Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature 425, 535-539.
Almeida, M. G., Macieira, S., Goncalves, L. L., Huber, R., Cunha, C. A., Romão, M. J., Costa, C., Lampreia, J., Moura, J. J. and I., M. (2003) The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774. Eur. J. Biochem. 270, 3904-3915.
Macieira, S., Martins, B. M. and Huber, R. (2003) Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation. FEMS Microbiol. Lett. 226, 31-37.
Jozic, D., Kaiser, J. T., Huber, R., Bode, W. and Maskos, K. (2003) X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases. J. Mol. Biol. 332, 243-256.
Gerhardt, S., Echt, S., Busch, M., Freigang, J., Auerbach, G., Bader, G., Martin, W. F., Bacher, A., Huber, R. and Fischer, M. (2003) Structure and properties of an engineered transketolase from maize. Plant Physiology 132, 1941-1949.
Steinbacher, S., Schiffmann, S., Richter, G., Huber, R., Bacher, A. and Fischer, M. (2003) Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: Implications for the catalytic mechanism. J. Biol. Chem. 278, 42256-42265.
Blaesse, M., Kupke, T., Huber, R. and Steinbacher, S. (2003) Structure of MrsD, an FAD-binding protein of the HFCD family. Acta Cryst.D58, 1414-1421.
Wendt, K. S., Schall, I., Huber, R., Buckel, W. and Jacob, U. (2003) Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase. EMBO J. 22, 3493-3502.
Henrich, S., Cameron, A., Bourenkov, G. P., Kiefersauer, R., Huber, R., Lindberg, I., Bode, W. and Than, M. E. (2003) The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nature Struct. Biol. 10, 520-526.
Gaßel, M., Breitenlechner, C. B., Rüger, P., Jucknischke, U., Schneider, T., Huber, R., Bossemeyer, D. and Engh, R. A. (2003) Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT). J. Mol. Biol. 329, 1021-1034.
Steinbacher, S., Kaiser, J., Gerhardt, S., Eisenreich, W., Huber, R., Bacher, A. and Rohdich, F. (2003) Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis. J. Mol. Biol. 329, 973-982.
Dobbek, H., Gremer, L., Meyer, O. and Huber, R. (2001) CO dehydrogenase. Handbook of Metalloproteins. A. Messerschmidt, R. Huber, T. Poulos and K. Wieghardt. Chichester, John Wiley & Sons,Ltd. 2: 1136-1147.
Declerck, N., Machius, M., Joyet, P., Wiegand, G., Huber, R. and Gaillardin, C. (2003) Hyperthermostabilization of bacillus licheniformis a-amylase and modulation of its stability over a 50oC temperature range. Protein Engineering 1647, 287-293.
Bae, J. H., Rubini, M., Jung, G., Wiegand, G., Seifert, M. H., Azim, M. K., Kim, J. S., Zumbusch, A., Holak, T. A., Moroder, L., Huber, R. and Budisa, N. (2003) Expansion of the genetic code enables design of a novel "Gold" class of green fluorescent proteins. J. Mol. Biol. 328, 1071-1081.
Augustin, M. A., Reichert, A. S., Betat, H., Huber, R., Morl, M. and Steegborn, C. (2003) Crystal structure of the human CCA-adding enzyme: Insights into template-independent polymerization. J. Mol. Biol. 328, 985-994.
Groll, M. and Huber, R. (2003) Substrate access and processing by the 20S proteasome core particle. Int. J. of Biochem. & Cell Biol. 35, 606-616.
Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R., Huber, R., Bode, W., Demuth, H. U. and Brandstetter, H. (2003) The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc. Natl. Acad. Sci. USA 100, 5063-5068.
Messerschmidt, A., Worbs, M., Steegborn, C., Wahl, M. C., Huber, R., Laber, B. and Clausen, T. (2003) Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: Crystal structure of cystathionine g-lyase from yeast and intrafamiliar structure comparison. Biol. Chem. 384, 373-386.
Song, H. K., Bochtler, M., Azim, M. K., Hartmann, C., Huber, R. and Ramachandran, R. (2003) Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. ;Biophys. Chem. 100, 437-452.
Steinbacher, S., Hernández-Acosta, P., Bieseler, B., Blaesse, M., Huber, R., Culiáñez-Macià, F. A. and Kupke, T. (2003) Crystal Structure of the plant PPC decarboxylase AtHAL3a complexed with an Ene-thiol reaction intermediate. J. Mol. Biol. 327, 193-202.
Declerck, N., Machius, M., Joyet, P., Wiegand, G., Huber, R. and Gaillardin, C. (2002) Engineering the thermostability of Bacillus licheniformis a-amylase. ;Biologia, Bratislava57, 203-211.
Groll, M., Brandstetter, H., Bartunik, H., Bourenkow, G. and Huber, R. (2003) Investigations on the maturation and regulation of archaebacterial proteasomes. J. Mol. Biol. 327, 75-83.
Steinbacher, S., Kaiser, J., Eisenreich, W., Huber, R., Bacher, A. and Rohdich, F. (2003) Structural basis of fosmidomycin action revealed by the complex with IspC:Implications for the catalytic mechanism and anti-malaria drug development. ;J. Biol. Chem. 278, 18401-18407.
Cunha, C. A., Macieira, S., Dias, J. M., Almeida, G., Goncalves, L. L., Costa, C., Lampreia, J., Huber, R., Moura, J. J., I., M. and Romao, M. J. (2003) Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774: the relevance of the two calcium sites in the structure of the catalytic subunit (NrfA). ;J. Biol. Chem. 278, 17455-17465. ;
Soulimane, T., Kiefersauer, R. and Than, M. E. (2003) ;Ba3-Type cytochrome c oxidase from Thermus thermophilus: Purification, crystallization and crystal transformation. ;Membrane Protein Purification and Crystallization. C. Hunte, H. Schägger and G. v. Jagow. San Diego, Elsevier Science, USA: 229-251.
Bauer, S., Kemter, K., Bacher, A., Huber, R., Fischer, M. and Steinbacher, S. (2003) Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold. ;J. Mol. Biol. 326, 1463-1473.
Fischer, M., Haase, I., Kis, K., Meining, W., Ladenstein, R., Cushman, M., Schramek, N., Huber, R. and Bacher, A. (2003) Enzyme catalysis via control of activation entropy: Site-directed mutagenesis of 6,7-Dimethyl-8-ribityllumazine synthase. ;J. Mol. Biol. 326, 783-793.
Machius, M., Declerck, N., Huber, R. and Wiegand, G. (2003) Kinetic stabilization of Bacillus licheniformis a-amylase through introduction of hydrophobic residues at the surface. ;J. Biol. Chem. 278, 11546-11553.
Rebelo, J., Auerbach, G., Bader, G., Bracher, A., Nar, H., Hösl, C., Schramek, N., Kaiser, J., Bacher, A., Huber, R. and Fischer, M. (2003). Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I. ;J. Mol. Biol. 326, 503-516.
Krapp, S., Mimura, Y., Jefferis, R., Huber, R. and Sondermann, P. (2003) Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. ;J. Mol. Biol. 325, 979-989.
Kim, J. S., Groll, M., Musiol, H. J., Behrendt, R., Kaiser, M., Moroder, L., Huber, R. and Brandstetter, H. (2002) Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum. ;J. Mol. Biol. 324, 1041-1050.
Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R. and Meyer, O. (2002) Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proc. Natl. Acad. Sci. USA 99, 15971-15976.
Sichler, K., Kopetzki, E., Huber, R., Bode, W., Hopfner, K. P. and Brandstetter, H. (2003) Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop. ;J. Biol. Chem. 278, 4121-4126.
Rehm, T., Huber, R. and Holak, T. A. (2002) Application of NMR in structural proteomics: screening for proteins amenable to structural analysis. Structure 10, 1613-1618.
Einsle, O., Messerschmidt, A., Huber, R., Kroneck, P. M. and Neese, F. (2002) Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase. J. Am. Chem. Soc. 124, 11737-11745.
Budisa, N., Rubini, M., Bae, J. H., Weyher, E., Wenger, W., Golbik, R., Huber, R. and Moroder, L. (2002) Global replacement of tryptophan with aminotryptophans generates non-invasive protein-based optical pH sensors. Angew. Chem. Int. Ed. 41, 4066-4069.
Sichler, K., Hopfner, K. P., Kopetzki, E., Huber, R., Bode, W. and Brandstetter, H. (2002) The influence of residue 190 in the S1 site of trypsin-like serine proteases on substrate selectivity is universally conserved. FEBS Lett. 530, 220-224.
Kaiser, J. T., Bruno, S., Clausen, T., Huber, R., Schiaretti, F., Mozzarelli, A. and Kessler, D. (2003) Snapshots of the cystine lyase C-DES during catalysis - studies in solution and in the crystalline state. ;J. Biol. Chem. 278, 357-365.
Gerhardt, S., Schott, A., Kairies, N., Cushman, M., Illarionov, B., Eisenreich, W., Bacher, A., Huber, R., Steinbacher, S. and Fischer, M. (2002) Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine. ;Structure 10, 1371-1381.
Cushman, M., Yang, D., Mihalic, J. T., Chen, J., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. (2002) Incorporation of an amide into 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors results in an unexpected reversal of selectivity for riboflavin synthase vs lumazine synthase. J. Org. Chem. 67, 6871-6877.
Göttig, P., Groll, M., Kim, J. S., Huber, R. and Brandstetter, H. (2002) Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism. ;EMBO J. 21, 5343-5352.
Brandstetter, H., Kim, J. S., Groll, M., Göttig, P. and Huber, R. (2002) Structural basis for the processive protein degradation by Tricorn protease. ;Biol. Chem. 383, 1157-1165.
Raaijmakers, H., Macieira, S., Dias, J. M., Teixeira, S., Bursakov, S., Huber, R., Moura, J. J. G., Moura, I. and Romão, M. J. (2002) Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. ;Structure 10, 1261-1272.
Garrido-Franco, M., Laber, B., Huber, R. and Clausen, T. (2002) Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase: implications for substrate binding and catalysis. ;J. Mol. Biol. 321, 601-612.
Sichler, K., Banner, D. W., D'Arcy, A., Hopfner, K. P., Huber, R., Bode, W., Kresse, G. B., Kopetzki, E. and Brandstetter, H. (2002) Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions. ;J. Mol. Biol. 322, 591-603.
Fischer, M. J., Romisch, W., Schiffmann, S., Kelly, M., Oschkinat, H., Steinbacher, S., Huber, R., Eisenreich, W., Richter, G. and Bacher, A. (2002) Biosynthesis of riboflavin in Archaea. Studies on the mechanism of 3,4-dihydroxy-2-butanone 4-phosphate synthase of methanococcus jannaschii. J. Biol. Chem. 277, 41410-41416.
Steiner, T., Kaiser, J. T., Marinkovic, S., Huber, R. and Wahl, M. C. (2002) Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities. ;EMBO J. 21, 4641-4653.
Schramek, N., Bracher, A., Fischer, M., Auerbach, G., Nar, H., Huber, R. and Bacher, A. (2002) Reaction mechanism of GTP cyclohydrolase I: single turnover experiments using a kinetically competent reaction intermediate. ;J. Mol. Biol. 316, 829-837.
Jozic, D., Bourenkow, G., Bartunik, H., Scholze, H., Dive, V., Henrich, B., Huber, R., Bode, W. and Maskos, K. (2002) Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. ;Structure 10, 1097-1106.
Fischer, M., Haase, I., Feicht, R., Richter, G., Gerhardt, S., Changeux, J. P., Huber, R. and Bacher, A. (2002) Biosynthesis of riboflavin 6,7-Dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe. ;Eur. J. Biochem. 269, 519-526.
Braun, N., Meining, W., Hars, U., Fischer, M., Ladenstein, R., Huber, R., Bacher, A., Weinkauf, S. and Bachmann, L. (2002) Formation of metal nanoclusters on specific surface sites of protein molecules. ;J. Mol. Biol. 321, 341-353.
Marquardt, U., Zettl, F., Huber, R., Bode, W. and Sommerhoff, C. (2002) The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region. ;J. Mol. Biol. 321, 491-502.
Atzenhofer, W., Regelsberger, G., Jacob, U., Peschek, G., Furtmuller, P., Huber, R. and Obinger, C. (2002) The 2.0Å resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase. ;J. Mol. Biol. 321, 479-489.
Cushman, M., Yang, D., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. (2002) Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase. ;J. Org. Chem. 67, 5807-5816.
Cha, H., Kopetzki, E., Huber, R., Lanzendörfer, M. and Brandstetter, H. (2002) Structural basis of the adaptive molecular recognition by MMP9. ;J. Mol. Biol. 320, 1065-1079.
Groll, M., Nazif, T., Huber, R. and Bogyo, M. (2002) Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome. ;Chemistry & Biology 9, 655-662.
Friedrich, R., Steinmetzer, T., Huber, R., Stürzebecher, J. and Bode, W. (2002) The methyl group of Na(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage. ;J. Mol. Biol. 316, 869-874.
Ramachandran, R., Hartmann, C., Song, H. K., Huber, R. and Bochtler, M. (2002) Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY). ;Proc. Natl. Acad. Sci. USA 99, 7396-7401.
Comellas-Bigler, M., Fuentes-Prior, P., Maskos, M., Huber, R., Oyama, H., Uchida, K., Dunn, B. M., Oda, K. and Bode, W. (2002) The 1.4 Å crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase. ;Structure 10, 865-876.
Gerhardt, S., Haase, I., Steinbacher, S., Kaiser, J. T., Cushman, M., Bacher, A., Huber, R. and Fischer, M. (2002) The structural basis of riboflavion binding to Schizosaccharomyces pombe 6,7-Dimethyl-8-ribityllumazine synthase. ;J. Mol. Biol. 318, 1317-1329.
Than, M. E., Henrich, S., Huber, R., Ries, A., Mann, K., Kühn, K., Timpl, R., Bourenkov, G. P., Bartunik, H. D. and Bode, W. (2002) The 1.9-Å crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proc. Natl. Acad. Sci. USA 99, 6607-6612.
Seifert, M. H., Breitenlechner, C. B., Bossemeyer, D., Huber, R., Holak, T. A. and Engh, R. A. (2002) Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using 31P NMR spectroscopy. ;Biochemistry 41, 5968-5977.
Garrido-Franco, M., Ehlert, S., Messerschmidt, A., Marinkovic, S., Huber, R., Laber, B., Bourenkov, G. P. and Clausen, T. (2002) Structure and function of threonine synthase from yeast. ;J. Biol. Chem. 277, 12396-12405.
Köhler, A., Bajorek, M., Groll, M., Moroder, L., Rubin, D. M., Huber, R., Glickmann, M. and Finley, D. (2001) The substrate translocation channel of the proteasome. ;Biochimie 83, 325-332.
Dobbek, H. and Huber, R. (2002) ;The molybdenum and tungsten cofactors: a crystallographic view. ;metal ions in biological systems. A. Sigel and H. Sigel. New York, Marcel Dekker, Inc. 39: 227-263.
Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. and Clausen, T. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. ;Nature 416, 455-459.
Kaiser, M., Groll, M., Renner, C., Huber, R. and Moroder, L. (2002) The core structure of TMC-95A is a promising lead for reversible proteasome inhibition. ;Angew. Chem. Int. Ed. 41, 780-783.
Richardson , J. L., Fuentes-Prior, P., Sadler, J. E., Huber, R. and Bode, W. (2002) Characterization of the residues involved in the human a-thrombin-haemadin complex: an exosite II-binding inhibitor. Biochemistry 41, 2535-2542.
Grazulis, S., Deibert, M., Rimseliene, R., Skirgaila, R., Sasnauskas, G., Lagunavicius, A., Repin, V., Urbanke, C., Huber, R. and Siksnys, V. (2002) Crystal structure of the Bse634I restriction endonuclease: comparison of two enzymes recognizing the same DNA sequence. ;Nucleic Acids Research 30, 876-885.
Riedl, S. J., Fuentes-Prior, P., Renatus, M., Kairies, N., Krapp, S., Huber, R., Salvesen, G. S. and Bode, W. (2001) Structural basis for the activation of human procaspase-7. ;Proc. Natl . Acad. Sci. USA 98, 14790-14795.
Lang, R., Kocourek, A., Braun, M., Tschesche, H., Huber, R., Bode, W. and Maskos, K. (2001) Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 Å crystal structure. ;J. Mol. Biol. 312, 731-742.
Kairies, N., Beisel, H. G., Fuentes-Prior, P., Tsuda, R., Muta, T., Iwanaga, S., Bode, W., Huber, R. and Kawabata, S. (2001) The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems. ;Proc. Natl. Acad. Sci. USA 98, 13519-13524.
Bochtler, M., Song, H. K., Hartmann, C., Ramachandran, R. and Huber, R. (2001) The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale. ;J. Struct. Biol. 135, 281-293.
Song, H. K., Mulrooney, S. B., Huber, R. and Hausinger, R. P. (2001) Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation. ;J. Biol. Chem. 276, 49359-49364.
Brandstetter, H., Kim, J. S., Groll, M. and Huber, R. (2001) Crystal structure of the tricorn protease reveals a protein disassembly line. ;Nature 414, 466-470.
Macedo-Ribeiro, S., Martins, B. M., Pereira, P. J., Buse, G., Huber, R. and Soulimane, T. (2001) New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus. ;J Biol. Inorg. Chem.. 6, 663-674.
Martins, B. M., Grimm, B., Mock, H. P., Richter, G., Huber, R. and Messerschmidt, A. (2001) Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-rax analysis. ;Acta Cryst. Biological Crystallography D57, 1709-1711.
Martins, B. M., Grimm, B., Mock, H. P., Huber, R. and Messerschmidt, A. (2001) Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. ;J. Biol. Chem. 276, 44108-44116.
Steegborn, C., Danot, O., Huber, R. and Clausen, C. (2001) Crystal structure of transcription factor MaIT domain III: a novel helix repeat fold implicated in regulated oligomerization. ;Structure 9, 1051-1060.
Ullrich, T. C. and Huber, R. (2001) The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle. ;J. Mol. Biol. 313, 1117-1125.
Estébanez-Perpiña, E., Bayés, A., Vendrell, J., Jongsma, M. A., Bown, D. P., Gatehouse, J. A., Huber, R., Bode, W., Avilés, F. X. and Reverter, D. (2001) Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera. ;J. Mol. Biol. 313, 629-638.
Klein, C., Georges, G., Künkele, K. P., Huber, R., Engh, R. A. and Hansen, S. (2001) High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53. ;J. Biol. Chem. 276, 37390-37401.
Kawabata, S., Beisel, H. G., Huber, R., Bode, W., Gokudan, S., Muta, T., Tsuda, R., Koori, K., Kawahara, T., Seki, N., Mizunoe, Y., Wai, S. N. and Iwanaga, S. (2001) ;Role of tachylectins in host defense of the japanese horseshoe crab Tachypleus Tridentatus. ;Phylogenetic Perspectives on the Vertebrate Immune System. Beck, Kluwer Academic/Plenum Publishers: 195-202.
Groll, M., Koguchi, Y., Huber, R. and Kohno, J. (2001) Crystal structure of the 20 S proteasome: TMC-95A complex: a non-covalent proteasome inhibior. ;J. Mol. Biol. 311, 543-548.
Steegborn, C., Laber, B., Messerschmidt, A., Huber, R. and Clausen, T. (2001) Crystal structures of cystathionine g-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor. ;J. Mol. Biol. 311, 789-801.
Golbik, R., Budisa, N., Renner, C., Weyher-Stingl, E., Rahfeld, J. U., Huber, R., Fischer, G. and Moroder, L. (2001) Studies on folding of fluoroproline-substituted variants of Barstar. ;Nova Acta Leopoldina Supplementum 16, 59-60.
Wendt, K. S., Vodermaier, H. C., Jacob, U., Gieffers, C., Gmachl, M., Peters, J. M., Huber, R. and Sondermann, P. (2001) Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex. Nature Struct. Biol. 8, 784-788.
Budisa, N., Alefelder, S., Bae, J. H., Golbik, R., Minks, C., Huber, R. and Moroder, L. (2001) Proteins with b-(thienopyrrolyl)alanines as alternative chromophores and pharmaceutically active amino acids. ;Protein Science 10, 1281-1292.
Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. and Meyer, O. (2001) Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. ;Science 293, 1281-1285.
Engh, R. A. and Huber, R. (2001) Structure quality and target parameters. ;International Tables for Crystallography, Volume F. Crystallography of Biological Macromolecules. M. G. Rossmann and E. Arnold. Dordrecht, The Netherlands, Kluwer Academic Publishers: 382-392.
Stubbs, M. T. and Huber, R. (2001) ;Isomorphous replacement. Locating heavy atom sites. ;International Tables for Crystallography, Volume F. Crystallography of Biological Macromolecules. M. G. Rossmann and E. Arnold. Dordrecht, The Netherlands, Kluwer Academic Publishers: 256-262.
Bae, J. H., Alefelder, S., Kaiser, J. T., Friedrich, R., Moroder, L., Huber, R. and Budisa, N. (2001) Incorporation of b-Selenolo[3,2-b]pyrrolyl-alanine into proteins for phase determination in protein X-ray crystallography. J. Mol. Biol. 309, 925-936.
Breitinger, U., Clausen, T., Ehlert, S., Huber, R., Laber, B., Schmidt, F., Pohl, E. and Messerschmidt, A. (2001) The three-dimensional structure of cystathionine b-lyase from Arabidopsis and its substrate specificity. ;Plant Physiology 126, 631-642.
Rebelo, J. M., Dias, J. M., Huber, R., Moura, J. J. G. and Romão, M. J. (2001) Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å. ;J. Biol. Inorg. Chem 6, 791-800.
Zeslawski, W., Beisel, H. G., Kamionka, M., Kalus, W., Engh, R. A., Huber, R., Lang, K. and Holak, T. A. (2001) The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5. ;EMBO J. 20, 3638-3644.
Worbs, M., Bourenkov, G. P., Bartunik, H., Huber, R. and Wahl, M. C. (2001) An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. ;Molecular Cell 7, 1177-1189.
Brandstetter, H., Grams, F., Glitz, D., Lang, A., Huber, R., Bode, W., Krell, H. W. and Engh, R. A. (2001) The 1.8- Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition. ;J. Biol. Chem. 276, 17405-17412.
Breithaupt, C., Strassner, J., Breitinger, U., Huber, R., Macheroux, P., Schaller, A. and Clausen, T. (2001) X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. ;Structure 9, 419-429.
Schaschke, N., Loidl, G., Groll, M., Matschiner, G., Zettl, F., Sommerhoff, C. P., Marquardt, U., Bode, W., Huber, R. and Moroder, L. (2001) Multivalent Inhibition of Eukaryotic Proteasome and Human b-tryptase. ;Peptides 2000. J. Martinez and J. A. Fehrentz. Paris, EDK: 7-13.
Renner, C., Alefelder, S., Bae, J. H., Budisa, N., Huber, R. and Moroder, L. (2001) Fluoroprolines as tools for protein design and engineering. ;Angew. Chem. Int. Ed. 40, 923-925.
Garrido-Franco, M., Laber, B., Huber, R. and Clausen, T. (2001) Structural basis for the function of pyridoxine 5'- phosphate synthase. Structure 9, 245-253.
Ullrich, T. C., Blaesse, M. and Huber, R. (2001) Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation. EMBO J. 20, 316-329.