1oc6

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{{STRUCTURE_1oc6| PDB=1oc6 | SCENE= }}
{{STRUCTURE_1oc6| PDB=1oc6 | SCENE= }}
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'''STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION'''
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===STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION===
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==Overview==
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The enzymatic digestion of cellulose entails intimate involvement of cellobiohydrolases, whose characteristic active-center tunnel contributes to a processive degradation of the polysaccharide. The cellobiohydrolase Cel6A displays an active site within a tunnel formed by two extended loops, which are known to open and close in response to ligand binding. Here we present five structures of wild-type and mutant forms of Cel6A from Humicola insolens in complex with nonhydrolyzable thio-oligosaccharides, at resolutions from 1.7-1.1 A, dissecting the structural accommodation of a processing substrate chain through the active center during hydrolysis. Movement of ligand is facilitated by extensive solvent-mediated interactions and through flexibility in the hydrophobic surfaces provided by a sheath of tryptophan residues.
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{{ABSTRACT_PUBMED_12842048}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Processive mechanism]]
[[Category: Processive mechanism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:39:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:30:26 2008''

Revision as of 12:30, 27 July 2008

Image:1oc6.png

Template:STRUCTURE 1oc6

STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 12842048

About this Structure

1OC6 is a Single protein structure of sequence from Humicola insolens. Full crystallographic information is available from OCA.

Reference

Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens., Varrot A, Frandsen TP, von Ossowski I, Boyer V, Cottaz S, Driguez H, Schulein M, Davies GJ, Structure. 2003 Jul;11(7):855-64. PMID:12842048

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