ArticleProceedings of the National Academy of Sciences of the United States of America2016
F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed.
- Enhanced Sampling of Protein Conformations in AlphaFold3 with Repulsive Bias in the Diffusion Generative Model.JACS Au · 2026Article
- A minimal chemo-mechanical Markov model for rotary catalysis of FNature communications · 2026Article
- The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Direct identification of the rotary angle of ATP cleavage in FBiophysical journal · 2023Article
- Reversible binding of divalent cations toFrontiers in molecular biosciences · 2023Review
- FFrontiers in microbiology · 2022Review
- Microsecond molecular dynamics suggest that a non-synonymous mutation, frequently observed in patients with mild symptoms in Tokyo, alters dynamics of the SARS-CoV-2 main protease.Biophysics and physicobiology · 2021Article
- Rotary catalysis of bovine mitochondrial FProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Single-molecule FRET methods to study the dynamics of proteins at work.Current opinion in biomedical engineering · 2019Article
- Insights into the origin of the high energy-conversion efficiency of FProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Insights into the mechanism of ATP-driven rotary motors from direct torque measurement.Biophysical reviews · 2019Review
- Single-molecule pull-out manipulation of the shaft of the rotary motor FScientific reports · 2019Article
- Motor torque measurement ofCommunications biology · 2019Article
- Multimodal Measurements of Single-Molecule Dynamics Using FluoRBT.Biophysical journal · 2018Article
- Article
- Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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7 authors.
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Abstract
Despite extensive studies, the structural basis for the mechanochemical coupling in the rotary molecular motor F1-ATPase (F1) is still incomplete. We performed single-molecule FRET measurements to monitor conformational changes in the stator ring-α3β3, while simultaneously monitoring rotations of the central shaft-γ. In the ATP waiting dwell, two of three β-subunits simultaneously adopt low FRET nonclosed forms. By contrast, in the catalytic intermediate dwell, two β-subunits are simultaneously in a high FRET closed form. These differences allow us to assign crystal structures directly to both major dwell states, thus resolving a long-standing issue and establishing a firm connection between F1 structure and the rotation angle of the motor. Remarkably, a structure of F1 in an ε-inhibited state is consistent with the unique FRET signature of the ATP waiting dwell, while most crystal structures capture the structure in the catalytic dwell. Principal component analysis of the available crystal structures further clarifies the five-step conformational transitions of the αβ-dimer in the ATPase cycle, highlighting the two dominant modes: the opening/closing motions of β and the loosening/tightening motions at the αβ-interface. These results provide a new view of tripartite coupling among chemical reactions, stator conformations, and rotary angles in F1-ATPase.
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