ArticleNature2015
Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
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Who cites it
136 citing papers in PubMed, 262 citations in OpenAlex.
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
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- Integrated physiological and transcriptomic analyses reveal that HmPIF1 overexpression confers lead stress tolerance in Hydrangea.Plant cell reports · 2026Article
- Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy.Nature communications · 2025Article
- Structures of rotary ATP synthase fromScience advances · 2025Article
- Structural dynamics of mitochondrial ATP synthase inbioRxiv : the preprint server for biology · 2025Article
- Engineering of ATP synthase for enhancement of proton-to-ATP ratio.Nature communications · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Symmetry breaking and mismatch in the torsional mechanism of ATP synthesis by FTheory in biosciences = Theorie in den Biowissenschaften · 2025Article
- Purification and Reconstitution of Ilyobacter tartaricus ATP Synthase.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Molecular Dynamics Simulations of the Mutated Proton-TransferringInternational journal of molecular sciences · 2024Article
- Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- ATP yield of plant respiration: potential, actual and unknown.Annals of botany · 2023Article
- Membrane Lipid Composition Influences the Hydration of Proton Half-Channels in FLife (Basel, Switzerland) · 2023Article
- Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?Frontiers in molecular biosciences · 2023Review
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Network representation and analysis of energy coupling mechanisms in cellular metabolism by a graph-theoretical approach.Theory in biosciences = Theorie in den Biowissenschaften · 2022Article
- Synthesis and Evaluation ofACS omega · 2022Article
- Structures ofScience (New York, N.Y.) · 2022Article
76 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP, the universal energy currency of cells, is produced by F-type ATP synthases, which are ancient, membrane-bound nanomachines. F-type ATP synthases use the energy of a transmembrane electrochemical gradient to generate ATP by rotary catalysis. Protons moving across the membrane drive a rotor ring composed of 8-15 c-subunits. A central stalk transmits the rotation of the c-ring to the catalytic F1 head, where a series of conformational changes results in ATP synthesis. A key unresolved question in this fundamental process is how protons pass through the membrane to drive ATP production. Mitochondrial ATP synthases form V-shaped homodimers in cristae membranes. Here we report the structure of a native and active mitochondrial ATP synthase dimer, determined by single-particle electron cryomicroscopy at 6.2 Å resolution. Our structure shows four long, horizontal membrane-intrinsic α-helices in the a-subunit, arranged in two hairpins at an angle of approximately 70° relative to the c-ring helices. It has been proposed that a strictly conserved membrane-embedded arginine in the a-subunit couples proton translocation to c-ring rotation. A fit of the conserved carboxy-terminal a-subunit sequence places the conserved arginine next to a proton-binding c-subunit glutamate. The map shows a slanting solvent-accessible channel that extends from the mitochondrial matrix to the conserved arginine. Another hydrophilic cavity on the lumenal membrane surface defines a direct route for the protons to an essential histidine-glutamate pair. Our results provide unique new insights into the structure and function of rotary ATP synthases and explain how ATP production is coupled to proton translocation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.