1ocj: Difference between revisions

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[[Image:1ocj.jpg|left|200px]]
{{Seed}}
[[Image:1ocj.png|left|200px]]


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{{STRUCTURE_1ocj|  PDB=1ocj  |  SCENE=  }}  
{{STRUCTURE_1ocj|  PDB=1ocj  |  SCENE=  }}  


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




==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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