The molecular structure of an axle-less F 1 -ATPase.
bioRxiv
; 2024 Aug 09.
Article
em En
| MEDLINE
| ID: mdl-39149353
ABSTRACT
F 1 F o ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F 1 -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 ß subunits. Cooperativity in F 1 -ATPase has long thought to be conferred through the γ subunit, with three key interaction sites between the γ and ß subunits being identified. Single molecule studies have demonstrated that the F 1 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 1 -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 ß subunit suggests that the complete γ subunit is important for coordinating efficient ATP binding of F 1 -ATPase.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
BioRxiv
Ano de publicação:
2024
Tipo de documento:
Article