1bvw

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[[Image:1bvw.gif|left|200px]]
[[Image:1bvw.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1bvw |SIZE=350|CAPTION= <scene name='initialview01'>1bvw</scene>, resolution 1.92&Aring;
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The line below this paragraph, containing "STRUCTURE_1bvw", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ACI:Catalytic+Proton+Donor+(Experimental)'>ACI</scene>, <scene name='pdbsite=BAS:Catalytic+Base+(Proposed)'>BAS</scene> and <scene name='pdbsite=MOD:Pka+Modulator'>MOD</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1bvw| PDB=1bvw | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvw OCA], [http://www.ebi.ac.uk/pdbsum/1bvw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bvw RCSB]</span>
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}}
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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.]]
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[[Category: cellobiohydrolase]]
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[[Category: Cellobiohydrolase]]
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[[Category: cellulase]]
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[[Category: Cellulase]]
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[[Category: cellulose degradation]]
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[[Category: Cellulose degradation]]
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[[Category: glycoside hydrolase family 6]]
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[[Category: Glycoside hydrolase family 6]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:01:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:18 2008''
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Revision as of 09:01, 2 May 2008

Template:STRUCTURE 1bvw

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

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