| http://purl.uniprot.org/citations/26460036 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26460036 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26460036 | http://www.w3.org/2000/01/rdf-schema#comment | "The structure of the intact ATP synthase from the α-proteobacterium Paracoccus denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray crystallography at 4.0 Å resolution. The ζ-protein is bound via its N-terminal α-helix in a catalytic interface in the F1 domain. The bacterial F1 domain is attached to the membrane domain by peripheral and central stalks. The δ-subunit component of the peripheral stalk binds to the N-terminal regions of two α-subunits. The stalk extends via two parallel long α-helices, one in each of the related b and b' subunits, down a noncatalytic interface of the F1 domain and interacts in an unspecified way with the a-subunit in the membrane domain. The a-subunit lies close to a ring of 12 c-subunits attached to the central stalk in the F1 domain, and, together, the central stalk and c-ring form the enzyme's rotor. Rotation is driven by the transmembrane proton-motive force, by a mechanism where protons pass through the interface between the a-subunit and c-ring via two half-channels in the a-subunit. These half-channels are probably located in a bundle of four α-helices in the a-subunit that are tilted at ∼30° to the plane of the membrane. Conserved polar residues in the two α-helices closest to the c-ring probably line the proton inlet path to an essential carboxyl group in the c-subunit in the proton uptake site and a proton exit path from the proton release site. The structure has provided deep insights into the workings of this extraordinary molecular machine."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1517542112"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1517542112"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Montgomery M.G."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Montgomery M.G."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Walker J.E."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Walker J.E."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Leslie A.G."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Leslie A.G."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Morales-Rios E."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/author | "Morales-Rios E."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/pages | "13231-13236"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/pages | "13231-13236"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/title | "Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 A resolution."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/title | "Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 A resolution."xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/volume | "112"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://purl.uniprot.org/core/volume | "112"xsd:string |
| http://purl.uniprot.org/citations/26460036 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26460036 |
| http://purl.uniprot.org/citations/26460036 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26460036 |