F_O-F₁ coupling and symmetry mismatch in ATP synthase resolved in every F_O rotation step.

ABSTRACT: F_OF₁ ATP synthase, a ubiquitous enzyme that synthesizes most ATP in living cells, is composed of two rotary motors: a membrane-embedded proton-driven F_O motor and a catalytic F₁ motor. These motors share both central and peripheral stalks. Although both F_O and F₁ have pseudo-symmetric structures, their symmetries do not match. How symmetry mismatch is solved remains elusive because of the missing intermediate structures of the rotational steps. Here, for the case of Bacillus PS3 ATP synthases with three- and 10-fold symmetries in F₁ and F_O, respectively, we uncovered the mechanical couplings between F_O and F₁ at every 36° rotation step via molecular dynamics simulations and compara

SUBMITTER: Kubo S 

PROVIDER: S-EPMC10397808 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature