Direct observation of the rotation of F1-ATPase

@article{Noji1997DirectOO,
  title={Direct observation of the rotation of F1-ATPase},
  author={Hiroyuki Noji and Ryohei Yasuda and Masasuke Yoshida and Kazuhiko Kinosita},
  journal={Nature},
  year={1997},
  volume={386},
  pages={299-302}
}
Cells employ a variety of linear motors, such as myosin1–3, kinesin4 and RNA polymerase5, which move along and exert force on a filamentous structure. But only one rotary motor has been investigated in detail, the bacterial flagellum6 (a complex of about 100 protein molecules7). We now show that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion. A central rotor of radius ∼1 nm, formed by its γ-subunit, turns in a stator barrel of… 

Rotary F1-ATPase

The rotation of γ within hours is compatible with the spectroscopically detected blockade of rotation in the AMP-PNP-inhibited enzyme in the time-range of seconds.

Phosphate release coupled to rotary motion of F1-ATPase

Atomistic molecular dynamics simulations are used to construct a first atomistic conformation of the intermediate state following the 40° substep of rotary motion, and to study the timing and molecular mechanism of inorganic phosphate (Pi) release coupled to the rotation.

Single-molecule observation of rotation of F1-ATPase through microbeads.

The relationships between chemical and mechanical events are shown by imaging individual F(1) molecules under an optical microscope and a new scheme emerges: as soon as a catalytic site binds ATP, the gamma-subunit always turns the same face (interaction surface) to the beta hosting that site.

Linear and rotary molecular motors.

  • K. Kinosita
  • Biology, Physics
    Advances in experimental medicine and biology
  • 1998
The use of huge and small probes as described above should be useful in studies of protein machines in general, as a means of detecting conformational changes in a single protein molecule during function.

Single-molecule imaging of rotation of F1-ATPase.

None of the Rotor Residues of F1-ATPase Are Essential for Torque Generation

How subunit coupling produces the γ-subunit rotary motion in F1-ATPase

  • J. PuM. Karplus
  • Biology
    Proceedings of the National Academy of Sciences
  • 2008
A coarse-grained plastic network model is used to show at a residue level of detail how the conformational changes of the catalytic β-subunits act on the γ-subunit through repulsive van der Waals interactions to generate a torque that drives unidirectional rotation, as observed experimentally.

Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

It is shown by high-speed imaging that the 120° step consists of roughly 90° and 30° substeps, each taking only a fraction of a millisecond, which supports the binding-change model for ATP synthesis by reverse rotation of F1-ATPase.

Chemomechanical coupling of human mitochondrial F1-ATPase motor.

ATP-driven rotation of human mitochondrial F1 is reported, demonstrating that chemomechanical coupling angles of the γ-subunit are tuned during evolution.
...

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