2bod: Difference between revisions

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

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

~~==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.~~

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.

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==About this Structure==

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[[Category: Thermobifida fusca]]

[[Category: Tim a/b fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 20~~:34:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:46:41 2008''

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-[[Image:2bod.gif|left|200px]]
+{{Seed}}
+[[Image:2bod.png|left|200px]]
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 {{STRUCTURE_2bod|  PDB=2bod  |  SCENE=  }}
-'''CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE'''
+===CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A 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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:34:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:46:41 2008''