1bvw
From Proteopedia
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|PDB= 1bvw |SIZE=350|CAPTION= <scene name='initialview01'>1bvw</scene>, resolution 1.92Å | |PDB= 1bvw |SIZE=350|CAPTION= <scene name='initialview01'>1bvw</scene>, resolution 1.92Å | ||
|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> | |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> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Schulein, M.]] | [[Category: Schulein, M.]] | ||
[[Category: Varrot, A.]] | [[Category: Varrot, A.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MAN]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NAG]] | ||
[[Category: cellobiohydrolase]] | [[Category: cellobiohydrolase]] | ||
[[Category: cellulase]] | [[Category: cellulase]] | ||
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[[Category: glycoside hydrolase family 6]] | [[Category: glycoside hydrolase family 6]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:18 2008'' |
Revision as of 16:09, 30 March 2008
| |||||||
| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , , | ||||||
| Activity: | Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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