8QBY

Respiratory complex I from Paracoccus denitrificans in MSP2N2 nanodiscs

8QBY の概要

• エントリーDOI: 10.2210/pdb8qby/pdb
• EMDBエントリー: 18324
• 分子名称: NADH-quinone oxidoreductase subunit K, NADH:ubiquinone oxidoreductase 17.2 kD subunit, NADH-quinone oxidoreductase subunit A, ... (31 entities in total)
• 機能のキーワード: respiratory complex i, nadh:ubiquinone oxidoreductase, nanodiscs, oxidoreductase
• 由来する生物種: Paracoccus denitrificans PD1222; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 614708.85

構造登録者

Ivanov, B.S.,Bridges, H.R.,Hirst, J. (登録日: 2023-08-25, 公開日: 2024-09-11, 最終更新日: 2025-03-26)

主引用文献

Ivanov, B.S.,Bridges, H.R.,Jarman, O.D.,Hirst, J.
Structure of the turnover-ready state of an ancestral respiratory complex I.
Nat Commun, 15:9340-9340, 2024

PubMed Abstract: Respiratory complex I is pivotal for cellular energy conversion, harnessing energy from NADH:ubiquinone oxidoreduction to drive protons across energy-transducing membranes for ATP synthesis. Despite detailed structural information on complex I, its mechanism of catalysis remains elusive due to lack of accompanying functional data for comprehensive structure-function analyses. Here, we present the 2.3-Å resolution structure of complex I from the α-proteobacterium Paracoccus denitrificans, a close relative of the mitochondrial progenitor, in phospholipid-bilayer nanodiscs. Three eukaryotic-type supernumerary subunits (NDUFS4, NDUFS6 and NDUFA12) plus a novel L-isoaspartyl-O-methyltransferase are bound to the core complex. Importantly, the enzyme is in a single, homogeneous resting state that matches the closed, turnover-ready (active) state of mammalian complex I. Our structure reveals the elements that stabilise the closed state and completes P. denitrificans complex I as a unified platform for combining structure, function and genetics in mechanistic studies.

PubMed: 39472559
DOI: 10.1038/s41467-024-53679-3

実験手法

ELECTRON MICROSCOPY (2.3 Å)