6YNX

Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-subcomplex

これはPDB形式変換不可エントリーです。

6YNX の概要

• エントリーDOI: 10.2210/pdb6ynx/pdb
• EMDBエントリー: 10859
• 分子名称: subunit a, ATPTT5, ATPTT6, ... (29 entities in total)
• 機能のキーワード: mitochondria, atp synthase, fo-subcomplex, if1 dimer, membrane protein
• 由来する生物種: Tetrahymena thermophila; 詳細
• タンパク質・核酸の鎖数: 41
• 化学式量合計: 1183248.55

構造登録者

Kock Flygaard, R.,Muhleip, A.,Amunts, A. (登録日: 2020-04-14, 公開日: 2020-09-30, 最終更新日: 2025-10-01)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.5 Å)