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http://purl.uniprot.org/citations/36220811http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36220811http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36220811http://www.w3.org/2000/01/rdf-schema#comment"Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. The model consists of 25 subunits, including nine lineage-specific, as well as 36 lipids. The rotary mechanism is influenced by the divergent peripheral stalk, conferring a greater conformational flexibility. Proton transfer in the lumenal half-channel occurs via a chain of five ordered water molecules. The dimerization interface is formed by subunit-g that is critical for interactions but not for the catalytic activity. Although overall dimer architecture varies among eukaryotes, we find that subunit-g together with subunit-e form an ancestral oligomerization motif, which is shared between the trypanosomal and mammalian lineages. Therefore, our data defines the subunit-g/e module as a structural component determining ATP synthase oligomeric assemblies."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.org/dc/terms/identifier"doi:10.1038/s41467-022-33588-z"xsd:string
http://purl.uniprot.org/citations/36220811http://purl.org/dc/terms/identifier"doi:10.1038/s41467-022-33588-z"xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Gahura O."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Gahura O."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Panicucci B."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Panicucci B."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Zikova A."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Zikova A."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Jain M."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Jain M."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Amunts A."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Amunts A."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Hierro-Yap C."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Hierro-Yap C."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Hollaus D."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Hollaus D."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Muhleip A."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Muhleip A."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Slapnickova M."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/author"Slapnickova M."xsd:string
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/36220811http://purl.uniprot.org/core/date"2022"xsd:gYear