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Updated: Jun 16, 2025
10:39
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
29.8K
The molecular structure of an axle-less F1-ATPase
Emily J Furlong1,2, Ian-Blaine P Reininger-Chatzigiannakis1, Yi C Zeng1,3
1Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.
Biorxiv : the Preprint Server for Biology
|August 16, 2024
Summary
The F1-ATPase motor
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- F1F0 ATP synthase is a rotary motor generating ATP via proton motive force.
- F1-ATPase hydrolyzes ATP, involving conformational changes and the central gamma subunit rotation.
- Cooperativity in F1-ATPase is linked to gamma-beta subunit interactions.
Purpose of the Study:
- To investigate the role of the gamma subunit in F1-ATPase function.
- To elucidate the structural basis of ATP hydrolysis efficiency in axle-less F1-ATPase.
Main Methods:
- Cryogenic electron microscopy (cryo-EM) structure determination of axle-less Bacillus sp. PS3 F1-ATPase.
Main Results:
- The structure revealed an unexpected binding-dwell conformation.
- Absence of gamma subunit interactions with open beta subunits was observed.
- Axle-less F1-ATPase showed reduced efficiency in ATP hydrolysis.
Conclusions:
- The complete gamma subunit is crucial for coordinating efficient ATP binding in F1-ATPase.
- Structural insights explain the reduced efficiency of axle-less F1-ATPase.
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