Structural basis of unisite catalysis of bacterial F₀F₁-ATPase.

ABSTRACT: Adenosine triphosphate (ATP) synthases (F₀F₁-ATPases) are crucial for all aerobic organisms. F₁, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central γε rotor inside a cylinder made of α ₃ β ₃ in three different conformations (referred to as β _E, β _TP, and β _DP). In this study, we determined multiple cryo-electron microscopy structures of bacterial F₀F₁ exposed to different reaction conditions. The structures of nucleotide-depleted F₀F₁ indicate that the ε subunit directly forces β _TP to adopt a closed form independent of the nucleotide binding

SUBMITTER: Nakano A 

PROVIDER: S-EPMC9896953 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature