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-Structure paper
| タイトル | Cryo-EM structure of the entire mammalian F-type ATP synthase. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 27, Issue 11, Page 1077-1085, Year 2020 |
| 掲載日 | 2020年9月14日 |
著者 | Gergely Pinke / Long Zhou / Leonid A Sazanov / ![]() |
| PubMed 要旨 | The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain ...The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine. |
リンク | Nat Struct Mol Biol / PubMed:32929284 |
| 手法 | EM (単粒子) |
| 解像度 | 3.5 - 3.76 Å |
| 構造データ | EMDB-10573, PDB-6tt7: EMDB-11127, PDB-6za9: |
| 化合物 | ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-LHG: ![]() ChemComp-P5S: ![]() ChemComp-CDL: ![]() ChemComp-S12: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / ATP synthase / mitochondrial / respiratory chain / mammalian |
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