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Updated: Jan 15, 2026
08:40
Light-driven Molecular Motors on Surfaces for Single Molecular Imaging
Published on: March 13, 2019
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Structural basis for efficient Fo motor rotation revealed by MCMD simulation and structural analysis.
Shintaroh Kubo1, Hiroyuki Noji2
1Department of Applied Chemistry, Graduate School of Engineering, the University of Tokyo, Tokyo 113-0033, Japan.
Biophysical Journal
|October 8, 2025
Summary
Side-chain flexibility and half-channel asymmetry enhance ATP synthase rotation. These conserved features in the F o domain improve molecular motor efficiency, guiding synthetic rotary system design.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioenergetics
Background:
- ATP synthase's F o domain acts as a rotary motor, essential for cellular energy production.
- Proton translocation drives the rotation of the c-ring rotor, but efficiency principles are unclear.
Purpose of the Study:
- Investigate factors influencing the rotational efficiency of the F o domain.
- Elucidate the roles of side-chain flexibility and half-channel geometry in motor function.
Main Methods:
- Utilized hybrid molecular simulations, combining coarse-grained modeling and Monte Carlo methods.
- Analyzed conserved F o structures across different species.
Main Results:
- Side-chain flexibility at proton-binding sites significantly enhances rotational activity.
- Angular mismatch between proton uptake and release also promotes rotation.
- Conserved residue geometry and asymmetric half-channel design were observed.
Conclusions:
- Side-chain flexibility is a key design principle for efficient F o domain rotation.
- Conserved structural features optimize the rotary mechanism.
- Findings provide a basis for engineering artificial rotary systems.
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