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8U1H

Axle-less Bacillus sp. PS3 F1 ATPase mutant

Summary for 8U1H
Entry DOI10.2210/pdb8u1h/pdb
EMDB information41811
DescriptorATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (7 entities in total)
Functional Keywordsatpase, atp synthase, hydrolase
Biological sourceBacillus sp. PS3
More
Total number of polymer chains7
Total formula weight357416.13
Authors
Furlong, E.J.,Zeng, Y.C.,Brown, S.H.J.,Sobti, M.,Stewart, A.G. (deposition date: 2023-09-01, release date: 2024-09-11, Last modification date: 2024-10-30)
Primary citationFurlong, 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, :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: 39428050
DOI: 10.1016/j.bbabio.2024.149521
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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