8BQ6

Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)

これはPDB形式変換不可エントリーです。

8BQ6 の概要

• エントリーDOI: 10.2210/pdb8bq6/pdb
• EMDBエントリー: 16160 16161 16163 16166 16172
• 分子名称: NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH dehydrogenase subunit 4L, ... (69 entities in total)
• 機能のキーワード: plant, mitochondria, complex, membrane protein
• 由来する生物種: Arabidopsis thaliana (thale cress); 詳細
• タンパク質・核酸の鎖数: 67
• 化学式量合計: 1588153.38

構造登録者

Klusch, N.,Kuehlbrandt, W. (登録日: 2022-11-18, 公開日: 2023-05-10, 最終更新日: 2024-11-13)

主引用文献

Klusch, N.,Dreimann, M.,Senkler, J.,Rugen, N.,Kuhlbrandt, W.,Braun, H.P.
Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 angstrom resolution.
Nat.Plants, 9:142-156, 2023

PubMed Abstract: Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III with a co-purified ubiquinone in the Q site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane.

PubMed: 36585502
DOI: 10.1038/s41477-022-01308-6

実験手法

ELECTRON MICROSCOPY (2.8 Å)