ArticleBiophysical journal2015
Torque transmission mechanism via DELSEED loop of F1-ATPase.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Visualizing Single V-ATPase Rotation Using Janus Nanoparticles.Nano letters · 2024Article
- Visualizing Single V-ATPase Rotation Using Janus Nanoparticles.bioRxiv : the preprint server for biology · 2024Article
- Directed proton transfer from FBiophysical reviews · 2023Review
- Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.Protein science : a publication of the Protein Society · 2023Article
- Direct identification of the rotary angle of ATP cleavage in FBiophysical journal · 2023Article
- Beyond binding change: the molecular mechanism of ATP hydrolysis by FFrontiers in chemistry · 2023Article
- Computational Design of Inhibitors Targeting the Catalytic β Subunit ofAntibiotics (Basel, Switzerland) · 2022Article
- Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase.Biochimica et biophysica acta. Bioenergetics · 2019Article
- Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites.The Journal of biological chemistry · 2019Article
- The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018Review
- Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in FBiophysical journal · 2018Article
- ATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase.Nature communications · 2015Article
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Authors and funding
5 authors.
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Abstract
F1-ATPase (F1) is an ATP-driven rotary motor in which the three catalytic β subunits in the stator ring sequentially induce the unidirectional rotation of the rotary γ subunit. Many lines of evidence have revealed open-to-closed conformational transitions in the β subunit that swing the C-terminal domain inward. This conformational transition causes a C-terminal protruding loop with conserved sequence DELSEED to push the γ subunit. Previous work, where all residues of DELSEED were substituted with glycine to disrupt the specific interaction with γ and introduce conformational flexibility, showed that F1 still rotated, but that the torque was halved, indicating a remarkable impact on torque transmission. In this study, we conducted a stall-and-release experiment on F1 with a glycine-substituted DELSEED loop to investigate the impact of the glycine substitution on torque transmission upon ATP binding and ATP hydrolysis. The mutant F1 showed a significantly reduced angle-dependent change in ATP affinity, whereas there was no change in the equilibrium for ATP hydrolysis. These findings indicate that the DELSEED loop is predominantly responsible for torque transmission upon ATP binding but not for that upon ATP hydrolysis.
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