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http://purl.uniprot.org/citations/16429154http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16429154http://www.w3.org/2000/01/rdf-schema#comment"The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1046"xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/author"Clare D.K."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/author"Ranson N.A."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/author"Horwich A.L."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/author"Saibil H.R."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/author"Farr G.W."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/author"Houldershaw D."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/pages"147-152"xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/title"Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes."xsd:string
http://purl.uniprot.org/citations/16429154http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/16429154http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16429154
http://purl.uniprot.org/citations/16429154http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16429154
http://purl.uniprot.org/uniprot/#_P0A6F5-mappedCitation-16429154http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16429154
http://purl.uniprot.org/uniprot/#_P0A6F9-mappedCitation-16429154http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16429154
http://purl.uniprot.org/uniprot/P0A6F5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16429154
http://purl.uniprot.org/uniprot/P0A6F9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16429154