8AP9
rotor of the Trypanosoma brucei mitochondrial ATP synthase dimer
Summary for 8AP9
| Entry DOI | 10.2210/pdb8ap9/pdb |
| EMDB information | 15562 |
| Descriptor | ATP synthase gamma subunit, ATP synthase, epsilon chain, putative, ATP synthase subunit epsilon, mitochondrial, ... (5 entities in total) |
| Functional Keywords | atp synthase, mitochondria, membrane protein |
| Biological source | Trypanosoma brucei brucei More |
| Total number of polymer chains | 13 |
| Total formula weight | 187824.92 |
| Authors | Muehleip, A.,Gahura, O.,Zikova, A.,Amunts, A. (deposition date: 2022-08-09, release date: 2022-10-26, Last modification date: 2024-07-24) |
| Primary citation | Gahura, O.,Muhleip, A.,Hierro-Yap, C.,Panicucci, B.,Jain, M.,Hollaus, D.,Slapnickova, M.,Zikova, A.,Amunts, A. An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases. Nat Commun, 13:5989-5989, 2022 Cited by PubMed Abstract: Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. The model consists of 25 subunits, including nine lineage-specific, as well as 36 lipids. The rotary mechanism is influenced by the divergent peripheral stalk, conferring a greater conformational flexibility. Proton transfer in the lumenal half-channel occurs via a chain of five ordered water molecules. The dimerization interface is formed by subunit-g that is critical for interactions but not for the catalytic activity. Although overall dimer architecture varies among eukaryotes, we find that subunit-g together with subunit-e form an ancestral oligomerization motif, which is shared between the trypanosomal and mammalian lineages. Therefore, our data defines the subunit-g/e module as a structural component determining ATP synthase oligomeric assemblies. PubMed: 36220811DOI: 10.1038/s41467-022-33588-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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