2ZWN
Crystal structure of the novel two-domain type laccase from a metagenome
Summary for 2ZWN
| Entry DOI | 10.2210/pdb2zwn/pdb |
| Descriptor | two-domain type laccase, COPPER (II) ION, CU-O-CU LINKAGE, ... (5 entities in total) |
| Functional Keywords | laccase, muticopper oxidase, oxidoreductase |
| Biological source | metagenomes |
| Total number of polymer chains | 3 |
| Total formula weight | 115430.69 |
| Authors | Komori, H.,Miyazaki, K.,Higuchi, Y. (deposition date: 2008-12-17, release date: 2009-04-07, Last modification date: 2024-03-13) |
| Primary citation | 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., 583:1189-1195, 2009 Cited by PubMed 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. PubMed: 19285076DOI: 10.1016/j.febslet.2009.03.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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