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PDBsum entry 2zwn
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Oxidoreductase
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PDB id
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2zwn
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References listed in PDB file
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Key reference
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Title
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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
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H.Komori,
K.Miyazaki,
Y.Higuchi.
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Ref.
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Febs Lett, 2009,
583,
1189-1195.
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PubMed id
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Abstract
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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.
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