9io5

Cryo-EM structure of G1-ATPase dimer from Mycoplasma mobile gliding machinery

spinqualitylabelsall models 9io5, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9io5 is a 26 chain structure with sequence from Mesomycoplasma mobile. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Ligands: ADP, ATP, MG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6KIC8_MYCM1 Publication Abstract from PubMed 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)-beta 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. Dimeric assembly of F(1)-like ATPase for the gliding motility of Mycoplasma.,Toyonaga T, Kato T, Kawamoto A, Miyata T, Kawakami K, Fujita J, Hamaguchi T, Namba K, Miyata M Sci Adv. 2025 Feb 28;11(9):eadr9319. doi: 10.1126/sciadv.adr9319. Epub 2025 Feb , 26. PMID:40009674 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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