2bog

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[[Image:2bog.gif|left|200px]]
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{{STRUCTURE_2bog| PDB=2bog | SCENE= }}
{{STRUCTURE_2bog| PDB=2bog | SCENE= }}
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'''CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE'''
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===CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16185060 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16185060}}
==About this Structure==
==About this Structure==
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[[Category: Thermobifida fusca]]
[[Category: Thermobifida fusca]]
[[Category: Tim a/b fold]]
[[Category: Tim a/b fold]]
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Revision as of 16:35, 28 July 2008

Image: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-CELLOBIOSIDE

Template:ABSTRACT PUBMED 16185060

About this Structure

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

Reference

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

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