2FQF

Crystal Structures of E. coli Laccase CueO under different copper binding situations

2FQF の概要

• エントリーDOI: 10.2210/pdb2fqf/pdb
• 関連するPDBエントリー: 2FQD 2FQE 2FQG
• 分子名称: Blue copper oxidase cueO, COPPER (II) ION, CU-O-CU LINKAGE, ... (5 entities in total)
• 機能のキーワード: azurin-like domain, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P36649
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53945.59

構造登録者

Li, X.,Wei, Z.,Zhang, M.,Teng, M.,Gong, W. (登録日: 2006-01-18, 公開日: 2007-01-30, 最終更新日: 2024-03-13)

主引用文献

Li, X.,Wei, Z.,Zhang, M.,Peng, X.,Yu, G.,Teng, M.,Gong, W.
Crystal structures of E. coli laccase CueO at different copper concentrations.
Biochem.Biophys.Res.Commun., 354:21-26, 2007

PubMed Abstract: CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper.

PubMed: 17217912
DOI: 10.1016/j.bbrc.2006.12.116

実験手法

X-RAY DIFFRACTION (2 Å)