8U1H

Axle-less Bacillus sp. PS3 F1 ATPase mutant

Summary for 8U1H

• Entry DOI: 10.2210/pdb8u1h/pdb
• EMDB information: 41811
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (7 entities in total)
• Functional Keywords: atpase, atp synthase, hydrolase
• Biological source: Bacillus sp. PS3; More
• Total number of polymer chains: 7
• Total formula weight: 357416.13

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: 2024-11-20)

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

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

Experimental method

ELECTRON MICROSCOPY (3 Å)