Dimeric assembly of F₁-like ATPase for the gliding motility of <i>Mycoplasma</i>.

ABSTRACT: Rotary ATPases, including F₁F_O-, V₁V_O-, and A₁A_O-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, Mycoplasma mobile, a dimeric F₁-like ATPase forms a chain structure within the cell, which is proposed to drive the gliding motility. However, the mechanisms of force generation and transmission remain unclear. We determined the electron cryomicroscopy (cryo-EM) structure of the dimeric F₁-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F₁F_O-ATPases. The F₁-like ATPase unit associated by two subunits GliD and GliE was named G₁-ATPase as an R₁ do

SUBMITTER: Toyonaga T 

PROVIDER: S-EPMC11864180 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature