6TE0
Cryo-EM structure of Euglena gracilis mitochondrial ATP synthase, OSCP/F1/c-ring, rotational state 3
Summary for 6TE0
| Entry DOI | 10.2210/pdb6te0/pdb |
| EMDB information | 10473 |
| Descriptor | ATP synthase subunit alpha, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | mitochondria, atp synthase, membrane protein |
| Biological source | Euglena gracilis More |
| Total number of polymer chains | 23 |
| Total formula weight | 612441.08 |
| Authors | Muhleip, A.,Amunts, A. (deposition date: 2019-11-10, release date: 2019-11-27, Last modification date: 2024-05-22) |
| Primary citation | Muhleip, A.,McComas, S.E.,Amunts, A. Structure of a mitochondrial ATP synthase with bound native cardiolipin. Elife, 8:-, 2019 Cited by PubMed 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 , 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 . 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 (IF) binds in a mode that is different from human, but conserved in Trypanosomatids. PubMed: 31738165DOI: 10.7554/eLife.51179 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.92 Å) |
Structure validation
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