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Correlation between the conformational states of F(1)-ATPase as determined from its crystal structure and single-molecule rotation
F(1)-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the γ-subunit against the α(3)β(3) ring. The crystal structures of F(1), which provide the structural basis for the catalysis mechanism, have shown essentially 1 stable conformational state. In contrast, single-molecule st...
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| Hauptverfasser: | , , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
National Academy of Sciences
2008
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2603257/ https://ncbi.nlm.nih.gov/pubmed/19075235 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0805828106 |
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