1QLE

CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT

1QLE の概要

• エントリーDOI: 10.2210/pdb1qle/pdb
• 関連するPDBエントリー: 1AR1
• 分子名称: CYTOCHROME C OXIDASE POLYPEPTIDE I-BETA, MANGANESE (II) ION, DINUCLEAR COPPER ION, ... (12 entities in total)
• 機能のキーワード: oxidoreductase/immune system, complex (oxidoreductase-antibody), electron transport, transmembrane, cytochrome oxidase, antibody complex, oxidoreductase-immune system complex
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P98002 P08306 P06030; Cell inner membrane; Single-pass membrane protein: P77921
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 152419.56

構造登録者

Harrenga, A.,Michel, H. (登録日: 1999-08-30, 公開日: 1999-12-02, 最終更新日: 2024-10-23)

主引用文献

Harrenga, A.,Michel, H.
The Cytochrome C Oxidase from Paracoccus Denitrificans Does not Change the Metal Center Ligation Upon Reduction
J.Biol.Chem., 274:33296-, 1999

PubMed Abstract: Cytochrome c oxidase catalyzes the reduction of oxygen to water. This process is accompanied by the vectorial transport of protons across the mitochondrial or bacterial membrane ("proton pumping"). The mechanism of proton pumping is still a matter of debate. Many proposed mechanisms require structural changes during the reaction cycle of cytochrome c oxidase. Therefore, the structure of the cytochrome c oxidase was determined in the completely oxidized and in the completely reduced states at a temperature of 100 K. No ligand exchanges or other major structural changes upon reduction of the cytochrome c oxidase from Paracoccus denitrificans were observed. The three histidine Cu(B) ligands are well defined in the oxidized and in the reduced states. These results are hardly compatible with the "histidine cycle" mechanisms formulated previously.

PubMed: 10559205
DOI: 10.1074/JBC.274.47.33296

実験手法

X-RAY DIFFRACTION (3 Å)