EMD-10467

Single-particle
4.32 Å
EMD-10467 Deposition: 10/11/2019
Map released: 27/11/2019
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10467

Cryo-EM structure of Euglena gracilis mitochondrial ATP synthase, full dimer, rotational states 1

EMD-10467

Single-particle
4.32 Å
EMD-10467 Deposition: 10/11/2019
Map released: 27/11/2019
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Euglena gracilis
Sample: Euglena gracilis mitochondrial ATP synthase dimer
Fitted models: 6tdu (Avg. Q-score: 0.236)

Deposition Authors: Muhleip A , Amunts A
Structure of a mitochondrial ATP synthase with bound native cardiolipin.
Muhleip A , McComas SE, Amunts A
(2019) eLife , 8
PUBMED: 31738165
DOI: doi:10.7554/eLife.51179
ISSN: 2050-084X
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.