| http://purl.uniprot.org/citations/31439765 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31439765 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31439765 | http://www.w3.org/2000/01/rdf-schema#comment | "V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and Vo in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V1-Vo torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family."xsd:string |
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| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/author | "Zhou L."xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/author | "Zhou L."xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/author | "Sazanov L.A."xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/author | "Sazanov L.A."xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/pages | "eaaw9144"xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/pages | "eaaw9144"xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/title | "Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. ."xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/title | "Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase."xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/volume | "365"xsd:string |
| http://purl.uniprot.org/citations/31439765 | http://purl.uniprot.org/core/volume | "365"xsd:string |
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