The six steps of the complete F₁-ATPase rotary catalytic cycle.

ABSTRACT: F₁F_o ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalysis mechanism. Isolated F₁-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 F₁-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 F₁-ATPase. Each state shows three catalytic β-subunits in different conformations, establishing the complet

SUBMITTER: Sobti M 

PROVIDER: S-EPMC8333055 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature