1oc7
D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-TETRATHIO-ALPHA-D-CELLOPENTOSIDE AT 1.1 ANGSTROM RESOLUTION
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OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1OC7 is a [Single protein] structure of sequence from [Humicola insolens] with NAG, BGC, SGC, MA3, MG, ACT, DMF and GOL as [ligands]. Active as [Cellulose 1,4-beta-cellobiosidase], with EC number [3.2.1.91]. Structure known Active Site: ACI. Full crystallographic information is available from [OCA].
ReferenceReference
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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