8BA0

Drosophila melanogaster complex I in the Twisted state (Dm2)

8BA0 の概要

• エントリーDOI: 10.2210/pdb8ba0/pdb
• EMDBエントリー: 15937
• 分子名称: NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (51 entities in total)
• 機能のキーワード: mitochondrial complex i, respiratory complex i, nadh:ubiquinone oxidoreductase, ubiquinone, oxidoreductase
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• タンパク質・核酸の鎖数: 43
• 化学式量合計: 965756.30

構造登録者

Agip, A.N.A.,Chung, I.,Sanchez-Martinez, A.,Whitworth, A.J.,Hirst, J. (登録日: 2022-10-10, 公開日: 2023-01-18, 最終更新日: 2024-10-09)

主引用文献

Agip, A.A.,Chung, I.,Sanchez-Martinez, A.,Whitworth, A.J.,Hirst, J.
Cryo-EM structures of mitochondrial respiratory complex I from Drosophila melanogaster.
Elife, 12:-, 2023

PubMed Abstract: Respiratory complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from NADH oxidation by ubiquinone to drive protons across an energy-transducing membrane. is a candidate model organism for complex I due to its high evolutionary conservation with the mammalian enzyme, well-developed genetic toolkit, and complex physiology for studies in specific cell types and tissues. Here, we isolate complex I from and determine its structure, revealing a 43-subunit assembly with high structural homology to its 45-subunit mammalian counterpart, including a hitherto unknown homologue to subunit NDUFA3. The major conformational state of the enzyme is the mammalian-type 'ready-to-go' active resting state, with a fully ordered and enclosed ubiquinone-binding site, but a subtly altered global conformation related to changes in subunit ND6. The mammalian-type 'deactive' pronounced resting state is not observed: in two minor states, the ubiquinone-binding site is unchanged, but a deactive-type π-bulge is present in ND6-TMH3. Our detailed structural knowledge of complex I provides a foundation for new approaches to disentangle mechanisms of complex I catalysis and regulation in bioenergetics and physiology.

PubMed: 36622099
DOI: 10.7554/eLife.84424

実験手法

ELECTRON MICROSCOPY (3.68 Å)