Journal
ELIFE
Volume 8, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.51179
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Funding
- Stiftelsen for Strategisk Forskning [FFL15:0325]
- Ragnar Soderbergs stiftelse [M44/16]
- Vetenskapsradet [NT_2015-04107]
- Cancerfonden [2017/1041]
- H2020 European Research Council [ERC-2018-StG-805230]
- Knut och Alice Wallenbergs Stiftelse [2018.0080]
- European Molecular Biology Organization [ALTF 260-2017]
- European Molecular Biology Organization
- Swedish Foundation for Strategic Research (SSF) [FFL15-0325] Funding Source: Swedish Foundation for Strategic Research (SSF)
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The mitochondrial ATP synthase fuels eukaryotic cells with chemical energy. Here we report the cryo-EM structure of a divergent ATP synthase dimer from mitochondria of Euglena gracilis, a member of the phylum Euglenozoa that also includes human parasites. It features 29 different subunits, 8 of which are newly identified. The membrane region was determined to 2.8 angstrom resolution, enabling the identification of 37 associated lipids, including 25 cardiolipins, which provides insight into protein-lipid interactions and their functional roles. The rotor-stator interface comprises four membrane-embedded horizontal helices, including a distinct subunit a. The dimer interface is formed entirely by phylum-specific components, and a peripherally associated subcomplex contributes to the membrane curvature. The central and peripheral stalks directly interact with each other. Last, the ATPase inhibitory factor 1 (IF1) binds in a mode that is different from human, but conserved in Trypanosomatids.
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