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Updated: Feb 15, 2026
09:48
Construction and Operation of a Light-driven Gold Nanorod Rotary Motor System
Published on: June 30, 2018
9.3K
Structure and dynamics of rotary V1 motor
Hiroshi Ueno1, Kano Suzuki2, Takeshi Murata2,3
1Department of Applied Chemistry, Graduate School of Engineering, University of Tokyo, Tokyo, 113-8656, Japan. hueno@nojilab.t.u-tokyo.ac.jp.
Cellular and Molecular Life Sciences : CMLS
|February 2, 2018
Summary
V1-ATPase, a rotary motor, is now better understood through recent structural and single-molecule studies. These investigations reveal its conformational changes during ATP-driven rotation, offering new insights into its function.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Rotary ATPases are essential energy-converting molecular machines.
- F1-ATPase is well-characterized, but V1-ATPase structure and dynamics remain less understood.
- V1-ATPase plays crucial roles in cellular processes.
Purpose of the Study:
- To review recent structural and single-molecule studies on V1-ATPase.
- To elucidate the conformational changes during V1-ATPase rotation.
- To compare V1-ATPase with other rotary motors.
Main Methods:
- High-resolution structural studies (e.g., X-ray crystallography).
- Single-molecule biophysics techniques.
- Comparative analysis of rotary molecular motors.
Main Results:
- Recent studies provide high-resolution structures of V1-ATPase.
- Conformational changes in catalytic sites during ATP hydrolysis are detailed.
- Rotational dynamics and chemomechanical coupling mechanisms are illuminated.
Conclusions:
- V1-ATPase structural and dynamic knowledge has significantly advanced.
- Understanding V1-ATPase conformational changes is key to its function.
- Comparative insights highlight unique aspects of V1-ATPase among rotary motors.
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