Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.

ABSTRACT: F-ATP synthases use proton flow through the F_O domain to synthesize ATP in the F₁ domain. In Escherichia coli, the enzyme consists of rotor subunits γεc₁₀ and stator subunits (αβ)₃δab₂. Subunits c₁₀ or (αβ)₃ alone are rotationally symmetric. However, symmetry is broken by the b₂ homodimer, which together with subunit δa, forms a single eccentric stalk connecting the membrane embedded F_O domain with the soluble F₁ domain, and the central rotating and curved stalk composed of subunit γε. Although each of the three catalytic binding sites in (αβ)₃ catalyzes the same set of partial reactions in the time average, they might not be fully equivalent at any moment, because the structural symmetry is broken by con

SUBMITTER: Sielaff H 

PROVIDER: S-EPMC6384691 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature