Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
X-ray structure of a two-domain type laccase: a missing link in the evolution of multi-copper proteins.,Komori H, Miyazaki K, Higuchi Y FEBS Lett. 2009 Apr 2;583(7):1189-95. Epub 2009 Mar 11. PMID:19285076[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Komori H, Miyazaki K, Higuchi Y. X-ray structure of a two-domain type laccase: a missing link in the evolution of multi-copper proteins. FEBS Lett. 2009 Apr 2;583(7):1189-95. Epub 2009 Mar 11. PMID:19285076 doi:10.1016/j.febslet.2009.03.008
