1ocj

From Proteopedia

Revision as of 15:14, 18 December 2007

MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH A THIOPENTASACCHARIDE AT 1.3 ANGSTROM RESOLUTION

Overview

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.

About this Structure

1OCJ is a Single protein structure of sequence from Humicola insolens with NAG, BGC, SSG, SGC, MA3, MG and ACY as ligands. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Known structural/functional Site: . 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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