ArticleNature structural & molecular biology2012
Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Article
- Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy.Nature communications · 2025Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Electric Forces and ATP Synthesis.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Mitochondrial ATP generation is more proteome efficient than glycolysis.Nature chemical biology · 2024Article
- 1,3,8-Triazaspiro[4.5]decane Derivatives Inhibit Permeability Transition Pores through a FInternational journal of molecular sciences · 2023Article
- The mitochondrial permeability transition: Recent progress and open questions.The FEBS journal · 2022Review
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Mechanisms of membrane protein crystallization in 'bicelles'.Scientific reports · 2022Article
- ATP synthase FCellular and molecular life sciences : CMLS · 2022Review
- Cooperation amongeLife · 2022Article
- ATP Synthase KFunction (Oxford, England) · 2022Article
- Power Failure of Mitochondria and Oxidative Stress in Neurodegeneration and Its Computational Models.Antioxidants (Basel, Switzerland) · 2021Review
- ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.Nature communications · 2021Article
- Overcoming Radiation Resistance by Iron-Platinum Metal Alloy Nanoparticles in Human Copper Transport 1-Overexpressing Cancer Cells via Mitochondrial Disturbance.International journal of nanomedicine · 2021Article
- Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies ofLife (Basel, Switzerland) · 2020Review
- ATP synthase: Evolution, energetics, and membrane interactions.The Journal of general physiology · 2020Review
- Review
- Bedaquiline inhibits the yeast and human mitochondrial ATP synthases.Communications biology · 2020Article
- Mechanical inhibition of isolated VeLife · 2020Article
9 more citing papers are in PubMed but not listed here.
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7 authors.
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Abstract
The proton pore of the F(1)F(o) ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c(10) ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release.
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