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| [[Image:2nlr.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2nlr| PDB=2nlr | SCENE= }} | | {{STRUCTURE_2nlr| PDB=2nlr | SCENE= }} |
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| '''STREPTOMYCES LIVIDANS ENDOGLUCANASE (EC: 3.2.1.4) COMPLEX WITH MODIFIED GLUCOSE TRIMER'''
| | ===STREPTOMYCES LIVIDANS ENDOGLUCANASE (EC: 3.2.1.4) COMPLEX WITH MODIFIED GLUCOSE TRIMER=== |
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| ==Overview==
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| Glycoside hydrolases have been classified into over 66 families on the basis of amino acid sequence. Recently a number of these families have been grouped into "clans" which share a common fold and catalytic mechanism [Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696]. Glycoside hydrolase Clan GH-C groups family 11 xylanases and family 12 cellulases, which share the same jellyroll topology, with two predominantly antiparallel beta-sheets forming a long substrate-binding cleft, and act with net retention of anomeric configuration. Here we present the three-dimensional structure of a family 12 endoglucanase, Streptomyces lividans CelB2, in complex with a 2-deoxy-2-fluorocellotrioside. Atomic resolution (1.2 A) data allow clear identification of two distinct species in the crystal. One is the glycosyl-enzyme intermediate, with the mechanism-based inhibitor covalently linked to the nucleophile Glu 120, and the other a complex with the reaction product, 2-deoxy-2-fluoro-beta-D-cellotriose. The active site architecture of the complex provides insight into the double-displacement mechanism of retaining glycoside hydrolases and also sheds light on the basis of the differences in specificity between family 12 cellulases and family 11 xylanases.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10200171}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10200171 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10200171}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glycosyl hydrolase]] | | [[Category: Glycosyl hydrolase]] |
| [[Category: Glycosyl-enzyme intermediate]] | | [[Category: Glycosyl-enzyme intermediate]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:37:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:12:41 2008'' |
