| Literature DB >> 19285076 |
Hirofumi Komori1, Kentaro Miyazaki, Yoshiki Higuchi.
Abstract
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.Entities:
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Year: 2009 PMID： 19285076 DOI： 10.1016/j.febslet.2009.03.008
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124