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http://purl.uniprot.org/citations/32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32879423http://www.w3.org/2000/01/rdf-schema#comment"In higher plants, chloroplast ATP synthase has a unique redox switch on its γ subunit that modulates enzyme activity to limit ATP hydrolysis at night. To understand the molecular details of the redox modulation, we used single-particle cryo-EM to determine the structures of spinach chloroplast ATP synthase in both reduced and oxidized states. The disulfide linkage of the oxidized γ subunit introduces a torsional constraint to stabilize the two β hairpin structures. Once reduced, free cysteines alleviate this constraint, resulting in a concerted motion of the enzyme complex and a smooth transition between rotary states to facilitate the ATP synthesis. We added an uncompetitive inhibitor, tentoxin, in the reduced sample to limit the flexibility of the enzyme and obtained high-resolution details. Our cryo-EM structures provide mechanistic insight into the redox modulation of the energy regulation activity of chloroplast ATP synthase."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.org/dc/terms/identifier"doi:10.1038/s42003-020-01221-8"xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/author"Fromme P."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/author"Williams D."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/author"Yang J.H."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/author"Kandiah E."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/author"Chiu P.L."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/name"Commun Biol"xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/pages"482"xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/title"Structural basis of redox modulation on chloroplast ATP synthase."xsd:string
http://purl.uniprot.org/citations/32879423http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/32879423http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32879423
http://purl.uniprot.org/citations/32879423http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32879423
http://purl.uniprot.org/uniprot/#_P00825-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P00833-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P06450-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P06451-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P06453-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P05435-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P11402-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P69447-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/#_P31853-mappedCitation-32879423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32879423
http://purl.uniprot.org/uniprot/P06450http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32879423