2ZWN: Crystal Structure Of The Novel Two-Domain Type Laccase From A Metagenome

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.
PDB ID: 2ZWNDownload
MMDB ID: 70660
PDB Deposition Date: 2008/12/17
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 2ZWN: trimeric; determined by author and by software (PISA)
Molecular Components in 2ZWN
Label Count Molecule
Proteins (3 molecules)
Two-domain Type Laccase
Molecule annotation
Chemicals (10 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB