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Updated: Sep 25, 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 ATP synthase under strain during catalysis
Hui Guo1,2, John L Rubinstein3,4,5
1Molecular Medicine Program, The Hospital for Sick Children, Toronto, Ontario, Canada.
Nature Communications
|April 26, 2022
Summary
Mitochondrial ATP synthases use a peripheral stalk that deforms under strain during ATP hydrolysis. This stalk
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- ATP synthases are crucial molecular machines that generate cellular energy.
- These machines comprise F1 and FO motors that drive ATP hydrolysis or proton translocation.
- A peripheral stalk stabilizes the F1 and FO motors, counteracting their opposing forces on a shared rotor.
Purpose of the Study:
- To investigate the structural dynamics of the peripheral stalk in yeast mitochondrial ATP synthase during rotary catalysis.
- To understand how the peripheral stalk withstands mechanical forces generated during ATP synthesis and hydrolysis.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was employed to visualize yeast mitochondrial ATP synthase.
- Imaging was performed under strain conditions during ATP-hydrolysis-driven rotary catalysis.
Main Results:
- Cryo-EM revealed significant deformation of the peripheral stalk under strain.
- The peripheral stalk actively opposes the bending forces exerted by the rotary motors.
- Strain accumulation in the stalk during proton translocation may drive rotor rotation in ATP synthesis.
Conclusions:
- The peripheral stalk plays a dynamic role in ATP synthase function, resisting mechanical stress.
- Stalk strain relaxation is proposed as a mechanism to drive the catalytic cycle of ATP synthesis.
- Understanding these dynamics offers insights into cellular energy production mechanisms.
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