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8BPX

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

これはPDB形式変換不可エントリーです。
8BPX の概要
エントリーDOI10.2210/pdb8bpx/pdb
関連するPDBエントリー8BED 8BEE 8BEF 8BEH 8BEL 8BEP
EMDBエントリー15998 15999 16000 16003 16007 16008 16153 16168
分子名称NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (76 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1641254.07
構造登録者
Klusch, N.,Kuehlbrandt, W. (登録日: 2022-11-18, 公開日: 2023-01-25, 最終更新日: 2024-11-06)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.09 Å)
構造検証レポート
Validation report summary of 8bpx
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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