{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kishikawa JI"],"funding":["MEXT | Japan Society for the Promotion of Science","MEXT | Japan Society for the Promotion of Science (JSPS)","Takeda Science Foundation"],"pagination":["9883"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11579504"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["ATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in the hydrophilic catalytic hexamer. However, the mechanism of how pmf converts into c-ring rotation remains unclear. This study presents a 2.8 Å cryo-EM structure of the V<sub>o</sub> domain of V/A-ATPase from Thermus thermophilus, revealing precise orientations of glutamate (Glu) residues in the c<sub>12</sub>-ring. Three Glu residues face a water channel, with one forming a salt bridge with the Arginine in the stator (a/Arg). Molecular dynamics (MD) simulations show that protonation of specific Glu residues triggers unidirectional Brownian motion of the c<sub>12</sub>-ring towards ATP synthes"],"journal":["Nature communications"],"pubmed_title":["Rotary mechanism of the prokaryotic V&lt;sub&gt;o&lt;/sub&gt; motor driven by proton motive force."],"pmcid":["PMC11579504"],"funding_grant_id":["23H02453","20K06514","22H02595"],"pubmed_authors":["Kishikawa JI","Nakano A","Mitsuoka K","Yokoyama K","Okazaki KI","Kato T","Nishida Y"],"additional_accession":[]},"is_claimable":false,"name":"Rotary mechanism of the prokaryotic V&lt;sub&gt;o&lt;/sub&gt; motor driven by proton motive force.","description":"ATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in the hydrophilic catalytic hexamer. However, the mechanism of how pmf converts into c-ring rotation remains unclear. This study presents a 2.8 Å cryo-EM structure of the V<sub>o</sub> domain of V/A-ATPase from Thermus thermophilus, revealing precise orientations of glutamate (Glu) residues in the c<sub>12</sub>-ring. Three Glu residues face a water channel, with one forming a salt bridge with the Arginine in the stator (a/Arg). Molecular dynamics (MD) simulations show that protonation of specific Glu residues triggers unidirectional Brownian motion of the c<sub>12</sub>-ring towards ATP synthes","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-03T01:07:30.966Z","creation":"2025-04-04T12:01:50.553Z"},"accession":"S-EPMC11579504","cross_references":{"pubmed":["39567487"],"doi":["10.1038/s41467-024-53504-x"]}}