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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]

1. Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, and Steitz TA. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J 1996 Nov 1; 15(21) 5739-51. pmid:8918451. PubMed HubMed [Tormo1996]
2. Shimon LJ, Bayer EA, Morag E, Lamed R, Yaron S, Shoham Y, and Frolow F. A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Structure 1997 Mar 15; 5(3) 381-90. pmid:9083107. PubMed HubMed [Shimon1997]
3. Hövel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, and Schomburg D. Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. EMBO J 2003 Oct 1; 22(19) 4922-32. doi:10.1093/emboj/cdg494 pmid:14517232. PubMed HubMed [Hovel2003]
4. Golan G, Shallom D, Teplitsky A, Zaide G, Shulami S, Baasov T, Stojanoff V, Thompson A, Shoham Y, and Shoham G. Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications. J Biol Chem 2004 Jan 23; 279(4) 3014-24. doi:10.1074/jbc.M310098200 pmid:14573597. PubMed HubMed [Golan2004]
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. Structure determination of the extracellular xylanase from Geobacillus stearothermophilus by selenomethionyl MAD phasing. Acta Crystallogr D Biol Crystallogr 2004 May; 60(Pt 5) 836-48. doi:10.1107/S0907444904004123 pmid:15103129. PubMed HubMed [Teplitsky2004]
6. Czjzek M, Ben David A, Bravman T, Shoham G, Henrissat B, and Shoham Y. Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus. J Mol Biol 2005 Nov 4; 353(4) 838-46. doi:10.1016/j.jmb.2005.09.003 pmid:16212978. PubMed HubMed [Czjzek2005]
7. Brüx C, Ben-David A, Shallom-Shezifi D, Leon M, Niefind K, Shoham G, Shoham Y, and Schomburg D. 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 May 26; 359(1) 97-109. doi:10.1016/j.jmb.2006.03.005 pmid:16631196. PubMed HubMed [Brux2006]
8. Alhassid A, Ben-David A, Tabachnikov O, Libster D, Naveh E, Zolotnitsky G, Shoham Y, and Shoham G. Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate. Biochem J 2009 Jul 29; 422(1) 73-82. doi:10.1042/BJ20090180 pmid:19505290. PubMed HubMed [Alhassid2009]