9IO5

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

9IO5 の概要

• エントリーDOI: 10.2210/pdb9io5/pdb
• EMDBエントリー: 60718
• 分子名称: G1-ATPase subunit beta, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total)
• 機能のキーワード: atpase, complex, kinase, ring, hydrolase
• 由来する生物種: Mycoplasma mobile 163K; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 1356534.82

構造登録者

Toyonaga, T.,Kato, T.,Kawamoto, A.,Miyata, T.,Kawakami, K.,Fujita, J.,Hamaguchi, T.,Namba, K.,Miyata, M. (登録日: 2024-07-08, 公開日: 2025-03-12)

主引用文献

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

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: 40009674
DOI: 10.1126/sciadv.adr9319

実験手法

ELECTRON MICROSCOPY (3.2 Å)