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==Overview== | ==Overview== | ||
Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Driguez, H.]] | [[Category: Driguez, H.]] | ||
[[Category: Dultz, E.]] | [[Category: Dultz, E.]] | ||
[[Category: Irwin, D | [[Category: Irwin, D C.]] | ||
[[Category: Jones, T | [[Category: Jones, T A.]] | ||
[[Category: Larsson, A | [[Category: Larsson, A M.]] | ||
[[Category: Roos, A.]] | [[Category: Roos, A.]] | ||
[[Category: Wilson, D | [[Category: Wilson, D B.]] | ||
[[Category: carbohydrate metabolism]] | [[Category: carbohydrate metabolism]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
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[[Category: tim a/b fold]] | [[Category: tim a/b fold]] | ||
''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 16:39:56 2008'' | ||
Revision as of 17:39, 21 February 2008
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CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE
OverviewOverview
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.
About this StructureAbout this Structure
2BOD is a Single protein structure of sequence from Thermobifida fusca. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Site: . 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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Cellulase
- Single protein
- Thermobifida fusca
- Bergfors, T.
- Driguez, H.
- Dultz, E.
- Irwin, D C.
- Jones, T A.
- Larsson, A M.
- Roos, A.
- Wilson, D B.
- Carbohydrate metabolism
- Cellulose degradation
- Endoglucanase
- Glycosidase
- Glycoside hydrolase family 6
- Hydrolase
- Methyl cellobiosyl-4-thio-beta-cellobioside
- Polysaccharide degradation
- Tim a/b fold