Structure of a mitochondrial ATP synthase with bound native cardiolipin.

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.

Alexey Amunts

Fellows programme

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


Publications 7.1.2