User:Yuval Shoham

Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in Geobacillus stearothermophilus and Clostridium thermocellum. He was involved in solving the crystal structures of:

• C. thermocellum cellulosomal CBD [1]
• C. thermocellum cohesin domain [2]
• G. stearothermophilus GH51 α-L-arabinofuranosidase [3]
• G. stearothermophilus GH67 α-glucuronidase [4]
• G. stearothermophilus GH10 β-xylanase [5]
• G. stearothermophilus GH39 β-xylosidase [6]
• G. stearothermophilus GH43 β-xylosidase [7]
• G. stearothermophilus GH43 1,5-α-L-arabinanase [8]

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1. Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, and Steitz TA. (1996). Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 1996;15(21):5739-51. | Google Books | Open Library
2. Shimon LJ, Bayer EA, Morag E, Lamed R, Yaron S, Shoham Y, and Frolow F. (1997). A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Structure. 1997;5(3):381-90. DOI:10.1016/s0969-2126(97)00195-0 |
3. Hövel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, and Schomburg D. (2003). Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. EMBO J. 2003;22(19):4922-32. DOI:10.1093/emboj/cdg494 |
4. Golan G, Shallom D, Teplitsky A, Zaide G, Shulami S, Baasov T, Stojanoff V, Thompson A, Shoham Y, and Shoham G. (2004). Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications. J Biol Chem. 2004;279(4):3014-24. DOI:10.1074/jbc.M310098200 |
5. Teplitsky A, Mechaly A, Stojanoff V, Sainz G, Golan G, Feinberg H, Gilboa R, Reiland V, Zolotnitsky G, Shallom D, Thompson A, Shoham Y, and Shoham G. (2004). Structure determination of the extracellular xylanase from Geobacillus stearothermophilus by selenomethionyl MAD phasing. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 5):836-48. DOI:10.1107/S0907444904004123 |
6. Czjzek M, Ben David A, Bravman T, Shoham G, Henrissat B, and Shoham Y. (2005). Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus. J Mol Biol. 2005;353(4):838-46. DOI:10.1016/j.jmb.2005.09.003 |
7. Brüx C, Ben-David A, Shallom-Shezifi D, Leon M, Niefind K, Shoham G, Shoham Y, and Schomburg D. (2006). The structure of an inverting GH43 beta-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues. J Mol Biol. 2006;359(1):97-109. DOI:10.1016/j.jmb.2006.03.005 |
8. Alhassid A, Ben-David A, Tabachnikov O, Libster D, Naveh E, Zolotnitsky G, Shoham Y, and Shoham G. (2009). Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate. Biochem J. 2009;422(1):73-82. DOI:10.1042/BJ20090180 |