1bvw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==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.
+
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==
==About this Structure==
Line 14: Line 14:
[[Category: Humicola insolens]]
[[Category: Humicola insolens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Davies, G.J.]]
+
[[Category: Davies, G J.]]
[[Category: Schulein, M.]]
[[Category: Schulein, M.]]
[[Category: Varrot, A.]]
[[Category: Varrot, A.]]
Line 26: Line 26:
[[Category: glycoside hydrolase family 6]]
[[Category: glycoside hydrolase family 6]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:04 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:38 2008''

Revision as of 09:59, 21 February 2008


1bvw, resolution 1.92Å

Drag the structure with the mouse to rotate

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 with , , and as ligands. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Known structural/functional Sites: , and . 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 Thu Feb 21 11:59:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools