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 (9)
ABSTRACT
Rotary ATPases, including F
1
F
O
-, V
1
V
O
-, and A
1
A
O
-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium,
Mycoplasma mobile
, a dimeric F
1
-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 F
1
-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F
1
F
O
-ATPases. The F
1
-like ATPase unit associated by two subunits GliD and GliE was named G
1
-ATPase as an R
1
domain of rotary ATPases. G
1
-β subunit, a homolog of the F
1
-ATPase catalytic subunit, exhibited a specific N-terminal region that incorporates the glycolytic enzyme, phosphoglycerate kinase into the complex. Structural features of the ATPase displayed strong similarities to F
1
-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G
1
-ATPase drives the
Mycoplasma
gliding motility.
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