1bvw
From Proteopedia
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[[Image:1bvw.gif|left|200px]] | [[Image:1bvw.gif|left|200px]] | ||
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'''CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS''' | '''CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS''' | ||
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[[Category: Schulein, M.]] | [[Category: Schulein, M.]] | ||
[[Category: Varrot, A.]] | [[Category: Varrot, A.]] | ||
- | [[Category: | + | [[Category: Cellobiohydrolase]] |
- | [[Category: | + | [[Category: Cellulase]] |
- | [[Category: | + | [[Category: Cellulose degradation]] |
- | [[Category: | + | [[Category: Glycoside hydrolase family 6]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:01:04 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:01, 2 May 2008
CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS
Overview
The three-dimensional structure of the catalytic core of the family 6 cellobiohydrolase II, Cel6A (CBH II), from Humicola insolens has been determined by X-ray crystallography at a resolution of 1.92 A. The structure was solved by molecular replacement using the homologous Trichoderma reesei CBH II as a search model. The H. insolens enzyme displays a high degree of structural similarity with its T. reesei equivalent. The structure features both O- (alpha-linked mannose) and N-linked glycosylation and a hexa-co-ordinate Mg2+ ion. The active-site residues are located within the enclosed tunnel that is typical for cellobiohydrolase enzymes and which may permit a processive hydrolysis of the cellulose substrate. The close structural similarity between the two enzymes implies that kinetics and chain-end specificity experiments performed on the H. insolens enzyme are likely to be applicable to the homologous T. reesei enzyme. These cast doubt on the description of cellobiohydrolases as exo-enzymes since they demonstrated that Cel6A (CBH II) shows no requirement for non-reducing chain-ends, as had been presumed. There is no crystallographic evidence in the present structure to support a mechanism involving loop opening, yet preliminary modelling experiments suggest that the active-site tunnel of Cel6A (CBH II) is too narrow to permit entry of a fluorescenyl-derivatized substrate, known to be a viable substrate for this enzyme.
About this Structure
1BVW is a Single protein structure of sequence from Humicola insolens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution., Varrot A, Hastrup S, Schulein M, Davies GJ, Biochem J. 1999 Jan 15;337 ( Pt 2):297-304. PMID:9882628 Page seeded by OCA on Fri May 2 12:01:04 2008