7L1R

PS3 F1-ATPase Hydrolysis Dwell

Summary for 7L1R

• Entry DOI: 10.2210/pdb7l1r/pdb
• EMDB information: 23115 23116 23117
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (6 entities in total)
• Functional Keywords: atpase, atp synthase, translocase
• Biological source: Bacillus sp. (strain PS3); More
• Total number of polymer chains: 7
• Total formula weight: 362851.34

Authors

Sobti, M.,Ueno, H.,Noji, H.,Stewart, A.G. (deposition date: 2020-12-15, release date: 2021-07-21, Last modification date: 2024-05-29)

Primary citation

Sobti, M.,Ueno, H.,Noji, H.,Stewart, A.G.
The six steps of the complete F 1 -ATPase rotary catalytic cycle.
Nat Commun, 12:4690-4690, 2021

PubMed Abstract: FF ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalysis mechanism. Isolated F-ATPase catalytic cores can hydrolyze ATP, passing through six intermediate conformational states to generate rotation of their central γ-subunit. Although previous structural studies have contributed greatly to understanding rotary catalysis in the F-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-ATPase. Each state shows three catalytic β-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-ATPase catalytic cycle.

PubMed: 34344897
DOI: 10.1038/s41467-021-25029-0

Experimental method

ELECTRON MICROSCOPY (3.1 Å)