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Mühleip A, McComas SE, Amunts A
Elife 8 (-) - [2019-11-18; online 2019-11-18]
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 Å 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.
Global Proteomics and Proteogenomics [Service]
PubMed 31738165
DOI 10.7554/eLife.51179
Crossref 10.7554/eLife.51179
pii: 51179
pmc: PMC6930080
PDB: 6TDU
PDB: 6TDV
PDB: 6TDW
PDB: 6TDX
PDB: 6TDY
PDB: 6TDZ
PDB: 6TE0