2bog: Difference between revisions

Revision as of 19:35, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2bog.png

Template:STRUCTURE 2bog

CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDECATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE

Template:ABSTRACT PUBMED 16185060

About this StructureAbout this Structure

2BOG is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion., Larsson AM, Bergfors T, Dultz E, Irwin DC, Roos A, Driguez H, Wilson DB, Jones TA, Biochemistry. 2005 Oct 4;44(39):12915-22. PMID:16185060

Page seeded by OCA on Mon Jul 28 19:35:56 2008

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OCA

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-[[Image:2bog.gif|left|200px]]
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 {{STRUCTURE_2bog|  PDB=2bog  |  SCENE=  }}
-'''CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE'''
+===CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE===
-==Overview==
+<!--
-Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 linkages in cellulose at accessible points along the polymer. The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside (Glc(2)-S-Glc(2)), has been determined to 1.5 A resolution. The glycosyl unit in subsite -1 was sterically hindered by Tyr73 and forced into a distorted (2)S(o) conformation. In the enzyme where Tyr73 was mutated to a serine residue, the hindrance was removed and the glycosyl unit in subsite -1 had a relaxed (4)C(1) chair conformation. The relaxed conformation was seen in two complex structures of the mutated enzyme, with cellotetrose (Glc(4)) at 1.64 A and Glc(2)-S-Glc(2) at 1.04 A resolution.
+The line below this paragraph, {{ABSTRACT_PUBMED_16185060}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16185060 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16185060}}
 ==About this Structure==
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 [[Category: Thermobifida fusca]]
 [[Category: Tim a/b fold]]
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