Structure of a mitochondrial ATP synthase with bound native cardiolipin

Elife. 2019 Nov 18;8:e51179. doi: 10.7554/eLife.51179.

Abstract

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.

Keywords: Euglena gracilis; Euglenozoa; algae; evolutionary biology; molecular biophysics; none; structural biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cardiolipins / chemistry*
  • Cardiolipins / metabolism*
  • Cryoelectron Microscopy
  • Euglena gracilis / enzymology*
  • Mitochondrial Proton-Translocating ATPases / chemistry*
  • Mitochondrial Proton-Translocating ATPases / metabolism*
  • Protein Binding
  • Protein Conformation

Substances

  • Cardiolipins
  • Mitochondrial Proton-Translocating ATPases

Associated data

  • PDB/6TDU
  • PDB/6TDV
  • PDB/6TDW
  • PDB/6TDX
  • PDB/6TDY
  • PDB/6TDZ
  • PDB/6TE0