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Updated: Dec 9, 2025
10:39
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
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Structure of the dimeric ATP synthase from bovine mitochondria
Tobias E Spikes1, Martin G Montgomery1, John E Walker2
1The Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
Summary
Bovine mitochondrial ATP synthase structure reveals proton uptake via a Grotthus mechanism. The peripheral stalk and wedge structures, including bound cardiolipin, are key to enzyme function and dimer assembly.
Area of Science:
- Biochemistry
- Structural Biology
- Mitochondrial Physiology
Background:
- ATP synthase is crucial for cellular energy production.
- Understanding its mechanism, especially proton transport, is vital.
- Previous structural data on dimeric ATP synthases may be inaccurate.
Purpose of the Study:
- To elucidate the structure of dimeric ATP synthase from bovine mitochondria in three rotational states.
- To investigate the mechanism of proton uptake and release.
- To characterize the peripheral stalk and wedge structures and their roles.
Main Methods:
- Electron cryo-microscopy (cryo-EM) was used to determine the structure.
- Analysis of enzyme architecture, mechanical properties, and subunit interactions.
Main Results:
- Evidence for a Grotthus mechanism in proton uptake via the inlet half channel.
- Detailed description of the peripheral stalk's role in damping rocking motions.
- Characterization of wedge structures, including bound cardiolipin and phospholipids, essential for monomer linkage and dimer formation.
- Identified structural differences with previous interpretations of porcine ATP synthase.
Conclusions:
- The Grotthus mechanism likely operates in proton transport across the mitochondrial membrane.
- The peripheral stalk and wedge structures are critical for ATP synthase function and stability.
- The bovine dimeric ATP synthase structure provides a more accurate model than previously proposed for porcine enzymes.
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