Yasuda, R., Masaike, T., Adachi, K., Noji, H., Itoh, H., Kinosita, K. (August 2003) The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer. Proceedings of the National Academy of Sciences of the United States of America, 100 (16). pp. 9314-8. ISSN 0027-8424
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Abstract
F1-ATPase is an ATP-driven rotary motor in which a rod-shaped gamma subunit rotates inside a cylinder made of alpha3beta3 subunits. To elucidate the conformations of rotating F1, we measured fluorescence resonance energy transfer (FRET) between a donor on one of the three betas and an acceptor on gamma in single F1 molecules. The yield of FRET changed stepwise at low ATP concentrations, reflecting the stepwise rotation of gamma. In the ATP-waiting state, the FRET yields indicated a gamma position approximately 40 degrees counterclockwise (= direction of rotation) from that in the crystal structures of mitochondrial F1, suggesting that the crystal structures mimic a metastable state before product release.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Adenosine Triphosphatases/chemistry Adenosine Triphosphate/ chemistry Bacillus/enzymology Crystallography, X-Ray Dose-Response Relationship, Drug Fluorescence Resonance Energy Transfer Models, Biological Models, Theoretical Mutation Protein Conformation Proton-Translocating ATPases/ chemistry |
| Subjects: | bioinformatics > genomics and proteomics > small molecules > ATP bioinformatics > genomics and proteomics > small molecules |
| CSHL Authors: | |
| Communities: | CSHL labs > Svoboda lab |
| Depositing User: | Matt Covey |
| Date: | 5 August 2003 |
| Date Deposited: | 11 Jun 2013 19:13 |
| Last Modified: | 10 Sep 2019 18:37 |
| PMCID: | PMC170915 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/27961 |
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