Entity ID: 21 ATPTT2 belongs to a great supramolecular entity Type III ATP synthase analyzed by Cryo-EM. The structure of ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a single ATPTT2 subunit at the dimer interface. ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1.ATPTT2 is a classical alpha/beta hydrolase fold, although with an inactive catalytic triad
Ligand
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Reference
Title: Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization Flygaard RK, Muhleip A, Tobiasson V, Amunts A Ref: Nat Commun, 11:5342, 2020 : PubMed
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(1). 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 A 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.
        
Representative scheme of AlphaBeta_hydrolase structure and an image from PDBsum server
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Databases
PDB-Sum
6YNX Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
6YNXFold classification based on Structure-Structure alignment of Proteins - FSSP server