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http://purl.uniprot.org/citations/10576729http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10576729http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10576729http://www.w3.org/2000/01/rdf-schema#comment"Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.org/dc/terms/identifier"doi:10.1126/science.286.5445.1700"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.org/dc/terms/identifier"doi:10.1126/science.286.5445.1700"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/author"Stock D."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/author"Stock D."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/author"Walker J.E."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/author"Walker J.E."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/author"Leslie A.G."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/author"Leslie A.G."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/pages"1700-1705"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/pages"1700-1705"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/title"Molecular architecture of the rotary motor in ATP synthase."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/title"Molecular architecture of the rotary motor in ATP synthase."xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/10576729http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/10576729http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10576729
http://purl.uniprot.org/citations/10576729http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10576729
http://purl.uniprot.org/citations/10576729http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10576729
http://purl.uniprot.org/citations/10576729http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10576729