Cryo-EM structure of the entire mammalian F-type ATP synthase

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00121456" target="_blank" >RIV/00216224:14740/20:00121456 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41594-020-0503-8" target="_blank" >https://www.nature.com/articles/s41594-020-0503-8</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41594-020-0503-8" target="_blank" >10.1038/s41594-020-0503-8</a>

Result language
angličtina
Original language name
Cryo-EM structure of the entire mammalian F-type ATP synthase
Original language description
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. Cryo-EM structures of the entire mammalian F1Fo ATPase reveal several new features and details on the proton translocation pathway and suggest a model for the opening of the permeability transition pore.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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