Dimeric assembly of F 1 -like ATPase for the gliding motility of Mycoplasma

• DOI: 10.1126/sciadv.adr9319
• Publication Date: 2025-02-26T18:58:46Z
• Authors: Takuma Toyonaga; Takayuki Kato; Akihiro Kawamoto; Tomoko Miyata; Keisuke Kawakami; Junso Fujita; Tasuku Hamaguchi; Keiichi Namba; Makoto Miyata
• Keywords: P-type ATPase; AAA proteins; Molecular motor; V-ATPase; F-ATPase; Gliding motility

Rotary ATPases, including F 1 O -, V and A -ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, Mycoplasma mobile , a dimeric -like ATPase forms chain structure within cell, which is proposed to drive motility. However, mechanisms of force generation transmission remain unclear. We determined electron cryomicroscopy (cryo-EM) complex. The revealed an assembly distinct from those -ATPases. unit associated by two subunits GliD GliE was named G -ATPase as R domain rotary ATPases. -β subunit, homolog catalytic exhibited specific N-terminal region incorporates glycolytic enzyme, phosphoglycerate kinase into Structural features displayed strong similarities -ATPase, suggesting rotation based on mechanism. Overall, cryo-EM provides insights mechanism through drives