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Structure of a mitochondrial ATP synthase with bound native cardiolipin
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab). Karolinska Institutet, Sweden.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab). Karolinska Institutet, Sweden.ORCID iD: 0000-0002-5302-1740
Number of Authors: 32019 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 8, article id e51179Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2019. Vol. 8, article id e51179
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Biological Sciences
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URN: urn:nbn:se:su:diva-177490DOI: 10.7554/eLife.51179ISI: 000504465500001PubMedID: 31738165OAI: oai:DiVA.org:su-177490DiVA, id: diva2:1385466
Available from: 2020-01-14 Created: 2020-01-14 Last updated: 2022-03-23Bibliographically approved

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Mühleip, AlexanderMcComas, Sarah E.Amunts, Alexey

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