Dimeric assembly of F<sub>1</sub>-like ATPase for the gliding motility of <i>Mycoplasma</i>.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 40009674.
- Also identified by DOI 10.1126/sciadv.adr9319 and PMC identifier 11864180.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Rotary ATPases, including F<sub>1</sub>F<sub>O</sub>-, V<sub>1</sub>V<sub>O</sub>-, and A<sub>1</sub>A<sub>O</sub>-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, <i>Mycoplasma mobile</i>, a dimeric F<sub>1</sub>-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<sub>1</sub>-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F<sub>1</sub>F<sub>O</sub>-ATPases. The F<sub>1</sub>-like ATPase unit associated by two subunits GliD and GliE was named G<sub>1</sub>-ATPase as an R<sub>1</sub> domain of rotary ATPases. G<sub>1</sub>-β subunit, a homolog of the F<sub>1</sub>-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<sub>1</sub>-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G<sub>1</sub>-ATPase drives the <i>Mycoplasma</i> gliding motility.
Medical subject headings
- Mycoplasma
- Protein Multimerization
- Proton-Translocating ATPases
- Bacterial Proteins