1oc6

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==Overview==
==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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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Boyer, V.]]
[[Category: Boyer, V.]]
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[[Category: Davies, G.J.]]
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[[Category: Davies, G J.]]
[[Category: Driguez, H.]]
[[Category: Driguez, H.]]
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[[Category: Frandsen, T.P.]]
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[[Category: Frandsen, T P.]]
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[[Category: Ossowski, I.Von.]]
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[[Category: Ossowski, I Von.]]
[[Category: Schulein, M.]]
[[Category: Schulein, M.]]
[[Category: Varrot, A.]]
[[Category: Varrot, A.]]
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[[Category: processive mechanism]]
[[Category: processive mechanism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:57 2008''

Revision as of 12:15, 21 February 2008


1oc6, resolution 1.50Å

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

1OC6 is a Single protein structure of sequence from Humicola insolens with , and 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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