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http://purl.uniprot.org/citations/12842048http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12842048http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12842048http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(03)00124-2"xsd:string
http://purl.uniprot.org/citations/12842048http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(03)00124-2"xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Davies G.J."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Davies G.J."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Varrot A."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Varrot A."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Driguez H."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Driguez H."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Frandsen T.P."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Frandsen T.P."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"von Ossowski I."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"von Ossowski I."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Cottaz S."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Cottaz S."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Boyer V."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Boyer V."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Schuelein M."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/author"Schuelein M."xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/12842048http://purl.uniprot.org/core/name"Structure"xsd:string