Structural highlights
FunctionA0A0M3VGF9_BACP3 Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] Publication Abstract from PubMedF(1)F(o) ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalysis mechanism. Isolated F(1)-ATPase catalytic cores can hydrolyze ATP, passing through six intermediate conformational states to generate rotation of their central gamma-subunit. Although previous structural studies have contributed greatly to understanding rotary catalysis in the F(1)-ATPase, the structure of an important conformational state (the binding-dwell) has remained elusive. Here, we exploit temperature and time-resolved cryo-electron microscopy to determine the structure of the binding- and catalytic-dwell states of Bacillus PS3 F(1)-ATPase. Each state shows three catalytic beta-subunits in different conformations, establishing the complete set of six states taken up during the catalytic cycle and providing molecular details for both the ATP binding and hydrolysis strokes. We also identify a potential phosphate-release tunnel that indicates how ADP and phosphate binding are coordinated during synthesis. Overall these findings provide a structural basis for the entire F(1)-ATPase catalytic cycle. The six steps of the complete F(1)-ATPase rotary catalytic cycle.,Sobti M, Ueno H, Noji H, Stewart AG Nat Commun. 2021 Aug 3;12(1):4690. doi: 10.1038/s41467-021-25029-0. PMID:34344897[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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