X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins
X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins
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DOI：
10.1016/j.febslet.2009.03.008
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发表时间：
2009-04-02
期刊：
影响因子：
3.5
通讯作者：
Higuchi, Yoshiki
中科院分区：
文献类型：
--
作者：
Komori, Hirofumi;Miyazaki, Kentaro;Higuchi, Yoshiki
从我们的内部元基因组数据库中鉴定出一个含有两个铜还蛋白类似结构域的多铜蛋白。重组蛋白mgLAC含有4个铜离子/亚基，可氧化多种酚类和非酚类底物，具有与普通漆酶相似的光谱性质。X-射线结构分析表明，该酶为同源三聚体结构，类似于亚硝酸盐还原酶(NIR)。然而，在结构域界面处发现了铜配位的差异。MgLAC在该位置包含一个T2/T3三核铜团簇，而在近红外光谱中，单核T2铜占据这个位置。因此，三聚体是双结构域多铜蛋白结构的重要组成部分，而mgLAC可能是近红外光谱的进化前体。(C)2009年欧洲生化学会联合会。爱思唯尔出版公司版权所有。
A multi-copper protein with two cupredoxin-like domains was identified from our in-house metagenomic database. The recombinant protein, mgLAC, contained four copper ions/subunits, oxidized various phenolic and non-phenolic substrates, and had spectroscopic properties similar to common laccases. X-ray structure analysis revealed a homotrimeric architecture for this enzyme, which resembles nitrite reductase (NIR). However, a difference in copper coordination was found at the domain interface. mgLAC contains a T2/T3 tri-nuclear copper cluster at this site, whereas a mononuclear T2 copper occupies this position in NIR. The trimer is thus an essential part of the architecture of two-domain multi-copper proteins, and mgLAC may be an evolutionary precursor of NIR. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.