3MK7

The structure of CBB3 cytochrome oxidase

3MK7 の概要

• エントリーDOI: 10.2210/pdb3mk7/pdb
• 分子名称: Cytochrome c oxidase, cbb3-type, subunit N, HEME C, HEXACYANOFERRATE(3-), ... (11 entities in total)
• 機能のキーワード: tm helices, oxidoreductase
• 由来する生物種: Pseudomonas stutzeri; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 462028.28

構造登録者

Buschmann, S.,Warkentin, E.,Michel, H.,Ermler, U. (登録日: 2010-04-14, 公開日: 2010-08-04, 最終更新日: 2024-11-06)

主引用文献

Buschmann, S.,Warkentin, E.,Xie, H.,Langer, J.D.,Ermler, U.,Michel, H.
The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping
Science, 329:327-330, 2010

PubMed Abstract: The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO--essential for the pathogenicity of many bacteria--that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations.

PubMed: 20576851
DOI: 10.1126/science.1187303

実験手法

X-RAY DIFFRACTION (3.2 Å)