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http://purl.uniprot.org/citations/11163218http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11163218http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11163218http://www.w3.org/2000/01/rdf-schema#comment"The type IV secretion system of Helicobacter pylori consists of 10--15 proteins responsible for transport of the transforming protein CagA into target epithelial cells. Secretion of CagA crucially depends on the hexameric ATPase, HP0525, a member of the VirB11-PulE family. We present the crystal structure of a binary complex of HP0525 bound to ADP. Each monomer consists of two domains formed by the N- and C-terminal halves of the sequence. ADP is bound at the interface between the two domains. In the hexamer, the N- and C-terminal domains form two rings, which together form a chamber open on one side and closed on the other. A model is proposed in which HP0525 functions as an inner membrane pore, the closure and opening of which is regulated by ATP binding and ADP release."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)00142-8"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)00142-8"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Savvides S.N."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Savvides S.N."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Waksman G."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Waksman G."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Lanka E."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Lanka E."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Herr A.B."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Herr A.B."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Yeo H.J."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/author"Yeo H.J."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/pages"1461-1472"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/pages"1461-1472"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/title"Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/title"Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system."xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/11163218http://purl.uniprot.org/core/volume"6"xsd:string