9AVJ
PS3 F1 ATPase Wild type
Summary for 9AVJ
| Entry DOI | 10.2210/pdb9avj/pdb |
| EMDB information | 43903 |
| Descriptor | ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (9 entities in total) |
| Functional Keywords | atpase, electron transfer, atp hydrolysis, membrane protein |
| Biological source | Bacillus sp. PS3 More |
| Total number of polymer chains | 7 |
| Total formula weight | 344359.06 |
| Authors | Sobti, M.,Stewart, A.G. (deposition date: 2024-03-03, release date: 2024-10-30, Last modification date: 2024-11-20) |
| Primary citation | Furlong, E.J.,Reininger-Chatzigiannakis, I.P.,Zeng, Y.C.,Brown, S.H.J.,Sobti, M.,Stewart, A.G. The molecular structure of an axle-less F 1 -ATPase. Biochim Biophys Acta Bioenerg, 1866:149521-149521, 2024 Cited by PubMed Abstract: FF ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F-ATPase catalytic cores can hydrolyse ATP, passing through a series of conformational states involving rotation of the central γ rotor subunit and the opening and closing of the catalytic β subunits. Cooperativity in F-ATPase has long thought to be conferred through the γ subunit, with three key interaction sites between the γ and β subunits being identified. Single molecule studies have demonstrated that the F complexes lacking the γ axle still "rotate" and hydrolyse ATP, but with less efficiency. We solved the cryogenic electron microscopy structure of an axle-less Bacillus sp. PS3 F-ATPase. The unexpected binding-dwell conformation of the structure in combination with the observed lack of interactions between the axle-less γ and the open β subunit suggests that the complete γ subunit is important for coordinating efficient ATP binding of F-ATPase. PubMed: 39428050DOI: 10.1016/j.bbabio.2024.149521 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.72 Å) |
Structure validation
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