We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1bvw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bvw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1bvw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bvw| PDB=1bvw | SCENE= }}
{{STRUCTURE_1bvw| PDB=1bvw | SCENE= }}
-
'''CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9882628}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9882628 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9882628}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Cellulose degradation]]
[[Category: Cellulose degradation]]
[[Category: Glycoside hydrolase family 6]]
[[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 Mon Jun 30 19:48:02 2008''

Revision as of 16:48, 30 June 2008

Image:1bvw.png

Template:STRUCTURE 1bvw

CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS

Template:ABSTRACT PUBMED 9882628

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 Mon Jun 30 19:48:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bvw"
Personal tools