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Cryo-EM structure of Euglena gracilis mitochondrial ATP synthase, OSCP/F1/c-ring in rotational state 1Cryo-EM structure of Euglena gracilis mitochondrial ATP synthase, OSCP/F1/c-ring in rotational state 1
Structural highlights
Publication Abstract from PubMedThe 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 A resolution, enabling the identification of 37 associated lipids, including 25 cardiolipins, which provides insight into protein-lipid interaction 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. Structure of a mitochondrial ATP synthase with bound native cardiolipin.,Muhleip A, McComas SE, Amunts A Elife. 2019 Nov 18;8. pii: 51179. doi: 10.7554/eLife.51179. PMID:31738165[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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