9IO5
Cryo-EM structure of G1-ATPase dimer from Mycoplasma mobile gliding machinery
Summary for 9IO5
| Entry DOI | 10.2210/pdb9io5/pdb |
| EMDB information | 60718 |
| Descriptor | G1-ATPase subunit beta, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | atpase, complex, kinase, ring, hydrolase |
| Biological source | Mycoplasma mobile 163K More |
| Total number of polymer chains | 26 |
| Total formula weight | 1356534.82 |
| Authors | Toyonaga, T.,Kato, T.,Kawamoto, A.,Miyata, T.,Kawakami, K.,Fujita, J.,Hamaguchi, T.,Namba, K.,Miyata, M. (deposition date: 2024-07-08, release date: 2025-03-12) |
| Primary citation | Toyonaga, T.,Kato, T.,Kawamoto, A.,Miyata, T.,Kawakami, K.,Fujita, J.,Hamaguchi, T.,Namba, K.,Miyata, M. Dimeric assembly of F 1 -like ATPase for the gliding motility of Mycoplasma. Sci Adv, 11:eadr9319-eadr9319, 2025 Cited by PubMed Abstract: 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. PubMed: 40009674DOI: 10.1126/sciadv.adr9319 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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