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X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins |
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| Authors: | Hirofumi Komori Kentaro Miyazaki Yoshiki Higuchi |
| Affiliation: | a Department of Life Science, Graduate School of Life Science, University of Hyogo and Himeji Institute of Technology, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan b RIKEN SPring-8 Center, 1-1-1 Koto, Mikazuki-cho, Sayo-gun, Hyogo 679-5248, Japan c Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan d Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan |
| 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. |
| Keywords: | Crystal structure Laccase Metagenome Molecular evolution Multi-copper protein Nitrite reductase |
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