Furlong, Emily J. and Reininger-Chatzigiannakis, Ian-Blaine P. and Zeng, Yi C. and Brown, Simon H.J. and Sobti, Meghna and Stewart, Alastair G. (2025) The molecular structure of an axle-less F1-ATPase. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1866 (1). p. 149521. ISSN 00052728
Full text not available from this repository.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 gamma rotor subunit and the opening and closing of the catalytic beta subunits. Cooperativity in F(1)-ATPase has long thought to be conferred through the gamma subunit, with three key interaction sites between the gamma and beta subunits being identified. Single molecule studies have demonstrated that the F(1) complexes lacking the gamma 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 gamma and the open beta subunit suggests that the complete gamma subunit is important for coordinating efficient ATP binding of F(1)-ATPase.
| Item Type: | Article |
|---|---|
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 05 May 2025 00:44 |
| Last Modified: | 05 May 2025 00:44 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/1657 |
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