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http://purl.uniprot.org/citations/22114184http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22114184http://www.w3.org/2000/01/rdf-schema#comment"V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V(1)-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A(3)B(3) complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1108810108"xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Arai S."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Murata T."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Shirouzu M."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Terada T."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Iwata S."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Saijo S."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Kakinuma Y."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Yamato I."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Ishizuka-Katsura Y."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Ohsawa N."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/author"Hossain K.M."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/pages"19955-19960"xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/title"Crystal structure of the central axis DF complex of the prokaryotic V-ATPase."xsd:string
http://purl.uniprot.org/citations/22114184http://purl.uniprot.org/core/volume"108"xsd:string
http://purl.uniprot.org/citations/22114184http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22114184
http://purl.uniprot.org/citations/22114184http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22114184
http://purl.uniprot.org/uniprot/#_P43435-mappedCitation-22114184http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22114184
http://purl.uniprot.org/uniprot/#_P43455-mappedCitation-22114184http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22114184