X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins

被引：41
|
作者：
Komori, Hirofumi [1 ,2 ,3 ]
Miyazaki, Kentaro [4 ,5 ]
Higuchi, Yoshiki [1 ,2 ,3 ]
机构：
[1] Hyogo Med Univ, Grad Sch Life Sci, Dept Life Sci, Kamigori, Hyogo 6781297, Japan
[2] Himeji Inst Technol, Kamigori, Hyogo 6781297, Japan
[3] RIKEN, SPring Ctr 8, Mikazuki, Hyogo 6795248, Japan
[4] Natl Inst Adv Ind Sci & Technol, Inst Biol Resources & Funct, Tsukuba, Ibaraki 3058566, Japan
[5] Univ Tokyo, Grad Sch Frontier Sci, Dept Med Genome Sci, Tsukuba, Ibaraki 3058566, Japan
来源：
FEBS LETTERS | 2009年 / 583卷 / 07期
基金：
日本学术振兴会;
关键词：
Crystal structure; Laccase; Metagenome; Molecular evolution; Multi-copper protein; Nitrite reductase; STREPTOMYCES-COELICOLOR; NITROSOMONAS-EUROPAEA; DIFFRACTION ANALYSIS; PHENOL OXIDASE; NITRITE; CRYSTALLIZATION; TOLERANCE; REDUCTASE; GENES; SITES;
D O I：
10.1016/j.febslet.2009.03.008
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：1189 / 1195
页数：7
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