6YNW

Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - central stalk/cring

Summary for 6YNW

• Entry DOI: 10.2210/pdb6ynw/pdb
• EMDB information: 10858
• Descriptor: subunit c, subunit gamma, subunit delta, ... (4 entities in total)
• Functional Keywords: mitochondria, atp synthase, central stalk, c-ring, membrane protein
• Biological source: Tetrahymena thermophila; More
• Total number of polymer chains: 13
• Total formula weight: 139631.05

Authors

Kock Flygaard, R.,Muhleip, A.,Amunts, A. (deposition date: 2020-04-14, release date: 2020-09-30, Last modification date: 2024-05-22)

Primary citation

Flygaard, R.K.,Muhleip, A.,Tobiasson, V.,Amunts, A.
Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
Nat Commun, 11:5342-5342, 2020

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 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.

PubMed: 33093501
DOI: 10.1038/s41467-020-18993-6

Experimental method

ELECTRON MICROSCOPY (3.1 Å)