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

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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. © 2009 Federation of European Biochemical Societies.

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Komori, H., Miyazaki, K., & Higuchi, Y. (2009). X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins. FEBS Letters, 583(7), 1189–1195. https://doi.org/10.1016/j.febslet.2009.03.008

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