Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
Journal, issue, pages	Nat Commun, Vol. 11, Issue 1, Page 5342, Year 2020
Publish date	Oct 22, 2020
Authors	Rasmus Kock Flygaard / Alexander Mühleip / Victor Tobiasson / Alexey Amunts /
PubMed Abstract	Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we ...Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 Å resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.
External links	Nat Commun / PubMed:33093501 / PubMed Central
Methods	EM (single particle)
Resolution	2.5 - 3.1 Å
Structure data	10857 6ynv EMDB-10857, PDB-6ynv: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-wing region Method: EM (single particle) / Resolution: 2.8 Å 10858 6ynw EMDB-10858, PDB-6ynw: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - central stalk/cring Method: EM (single particle) / Resolution: 3.1 Å 10859 6ynx EMDB-10859, PDB-6ynx: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-subcomplex Method: EM (single particle) / Resolution: 2.5 Å 10860 6yny EMDB-10860: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo dimer PDB-6yny: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo composite dimer model Method: EM (single particle) / Resolution: 2.7 Å 10861 6ynz EMDB-10861: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo tetramer PDB-6ynz: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo composite tetramer model Method: EM (single particle) / Resolution: 3.1 Å 10862 6yo0 EMDB-10862, PDB-6yo0: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1/peripheral stalk Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-NAD: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NADYM / Nicotinamide adenine dinucleotide ChemComp-CDL: CARDIOLIPIN / phospholipidYM / Cardiolipin ChemComp-PC1: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM / Phosphatidylcholine ChemComp-PO4: PHOSPHATE ION / Phosphate ChemComp-UQ8: Ubiquinone-8 ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-MG: Unknown entry ChemComp-PEE: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipidYM / Discrete optimized protein energy ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate
Source	tetrahymena thermophila (eukaryote)
Keywords	MEMBRANE PROTEIN / mitochondria / ATP synthase / oxidoreductase / NAD / central stalk / c-ring / Fo-subcomplex / IF1 dimer / F1Fo dimer / F1Fo tetramer / F1-subcomplex / peripheral stalk / IF1