PDBsum entry 2zwn

Oxidoreductase

PDB id: 2zwn

Contents

Protein chains

317 a.a. *

Ligands

C2O ×3

Metals

_CL

_CU ×6

Waters ×628

* Residue conservation analysis

PDB id:

2zwn

Name:

Oxidoreductase

Title:

Crystal structure of the novel two-domain type laccase from a metagenome

Structure:

Two-domain type laccase. Chain: a, b, c. Engineered: yes

Source:

Metagenomes. Organism_taxid: 408169. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.70Å R-factor: 0.161 R-free: 0.183

Authors:

H.Komori,K.Miyazaki,Y.Higuchi

Key ref:

H.Komori et al. (2009). X-ray structure of a two-domain type laccase: a missing link in the evolution of multi-copper proteins. Febs Lett, 583, 1189-1195. PubMed id: 19285076

Date:

17-Dec-08 Release date: 07-Apr-09

Protein chains

C0STU6  (C0STU6_9BACT) -  Multicopper oxidase from uncultured bacterium

Seq: 359 a.a.

Struc: 317 a.a.

Febs Lett 583:1189-1195 (2009)

PubMed id: 19285076

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

H.Komori, K.Miyazaki, Y.Higuchi.

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.