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TitleDimeric assembly of F-like ATPase for the gliding motility of .
Journal, issue, pagesSci Adv, Vol. 11, Issue 9, Page eadr9319, Year 2025
Publish dateFeb 28, 2025
AuthorsTakuma Toyonaga / Takayuki Kato / Akihiro Kawamoto / Tomoko Miyata / Keisuke Kawakami / Junso Fujita / Tasuku Hamaguchi / Keiichi Namba / Makoto Miyata /
PubMed AbstractRotary ATPases, including FF-, VV-, and AA-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, , a dimeric F-like ATPase forms a chain ...Rotary ATPases, including FF-, VV-, and AA-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, , a dimeric F-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-like ATPase complex. The structure revealed an assembly distinct from those of dimeric FF-ATPases. The F-like ATPase unit associated by two subunits GliD and GliE was named G-ATPase as an R domain of rotary ATPases. G-β subunit, a homolog of the F-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-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G-ATPase drives the gliding motility.
External linksSci Adv / PubMed:40009674 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

60718

9io5

EMDB-60718, PDB-9io5:
Cryo-EM structure of G1-ATPase dimer from Mycoplasma mobile gliding machinery
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-PO4:
PHOSPHATE ION

Source
  • mycoplasma mobile 163k (bacteria)
KeywordsHYDROLASE / ATPase / Complex / kinase / Ring

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