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Literature DB >> 9657145

F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps.

R Yasuda¹, H Noji, K Kinosita, M Yoshida.

Abstract

A single molecule of F1-ATPase, a portion of ATP synthase, is by itself a rotary motor in which a central gamma subunit rotates against a surrounding cylinder made of alpha3beta3 subunits. Driven by three catalytic betas, each fueled with ATP, gamma makes discrete 120 degree steps, occasionally stepping backward. The work done in each step is constant over a broad range of imposed load and is close to the free energy of hydrolysis of one ATP molecule.

Entities: Chemical Gene

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Year: 1998 PMID： 9657145 DOI： 10.1016/s0092-8674(00)81456-7

Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582

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Cited

210 in total

1. The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.

Authors: H Omote; N Sambonmatsu; K Saito; Y Sambongi; A Iwamoto-Kihara; T Yanagida; Y Wada; M Futai
Journal: Proc Natl Acad Sci U S A Date: 1999-07-06 Impact factor: 11.205

2. A maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes.

Authors: U A van der Heide; S C Hopkins; Y E Goldman
Journal: Biophys J Date: 2000-04 Impact factor: 4.033

3. Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site.

Authors: P H Kuo; R K Nakamoto
Journal: Biochem J Date: 2000-05-01 Impact factor: 3.857

F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps.

1. The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.

2. A maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes.

3. Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site.

4. The mechanochemistry of V-ATPase proton pumps.

Review 5. Structural model of F1-ATPase and the implications for rotary catalysis.

Review 6. How Fo-ATPase generates rotary torque.

Review 7. A rotary molecular motor that can work at near 100% efficiency.

8. Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging.

9. ATP synthase and other motor proteins.

10. Energy transduction in the sodium F-ATPase of Propionigenium modestum.