2nlr
From Proteopedia
(New page: 200px<br /><applet load="2nlr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nlr, resolution 1.20Å" /> '''STREPTOMYCES LIVIDAN...) |
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==Overview== | ==Overview== | ||
| - | Glycoside hydrolases have been classified into over 66 families on the | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
| - | [[Category: Davies, G | + | [[Category: Davies, G J.]] |
[[Category: Dupont, C.]] | [[Category: Dupont, C.]] | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
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[[Category: hydrolase (endoglucanase)]] | [[Category: hydrolase (endoglucanase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:18 2008'' |
Revision as of 16:08, 21 February 2008
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STREPTOMYCES LIVIDANS ENDOGLUCANASE (EC: 3.2.1.4) COMPLEX WITH MODIFIED GLUCOSE TRIMER
Overview
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.
About this Structure
2NLR is a Single protein structure of sequence from Streptomyces lividans. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution., Sulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, Davies GJ, Biochemistry. 1999 Apr 13;38(15):4826-33. PMID:10200171
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