PDBsum entry 4j3q

Oxidoreductase

PDB id: 4j3q

Contents

Protein chains

338 a.a.

Ligands

NAG-NAG

NAG ×3

Metals

_CU ×4

Waters ×2

PDB id:

4j3q

Name:

Oxidoreductase

Title:

Crystal structure of truncated catechol oxidase from aspergillus oryzae

Structure:

Catechol oxidase. Chain: a, b. Fragment: unp residues 70-408. Engineered: yes

Source:

Aspergillus oryzae. Yellow koji mold. Organism_taxid: 5062. Strain: vtt-d-88348. Gene: 5990879. Expressed in: trichoderma reesei. Expression_system_taxid: 51453.

Resolution:

2.90Å R-factor: 0.179 R-free: 0.248

Authors:

N.Hakulinen,C.Gasparetti,H.Kaljunen,J.Rouvinen

Key ref:

N.Hakulinen et al. (2013). The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae. J Biol Inorg Chem, 18, 917-929. PubMed id: 24043469 DOI: 10.1007/s00775-013-1038-9

Date:

06-Feb-13 Release date: 27-Nov-13

Protein chains

Q2UNF9  (Q2UNF9_ASPOR) -  Tyrosinase copper-binding domain-containing protein from Aspergillus oryzae (strain ATCC 42149 / RIB 40)

Seq: 408 a.a.

Struc: 338 a.a.

Enzyme reactions

• Enzyme class: E.C.1.10.3.1 - catechol oxidase.
• Reaction: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O

2 × catechol (Bound ligand (Het Group name = NAG) matches with 57.14% similarity) + O2 = 2 × 1,2-benzoquinone + 2 × H2O

• Cofactor: Cu cation

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1007/s00775-013-1038-9

J Biol Inorg Chem 18:917-929 (2013)

PubMed id: 24043469

The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae.

N.Hakulinen, C.Gasparetti, H.Kaljunen, K.Kruus, J.Rouvinen.

ABSTRACT

Catechol oxidases (EC 1.10.3.1) catalyse the oxidation of o-diphenols to their corresponding o-quinones. These oxidases contain two copper ions (CuA and CuB) within the so-called coupled type 3 copper site as found in tyrosinases (EC 1.14.18.1) and haemocyanins. The crystal structures of a limited number of bacterial and fungal tyrosinases and plant catechol oxidases have been solved. In this study, we present the first crystal structure of a fungal catechol oxidase from Aspergillus oryzae (AoCO4) at 2.5-Å resolution. AoCO4 belongs to the newly discovered family of short-tyrosinases, which are distinct from other tyrosinases and catechol oxidases because of their lack of the conserved C-terminal domain and differences in the histidine pattern for CuA. The sequence identity of AoCO4 with other structurally known enzymes is low (less than 30 %), and the crystal structure of AoCO4 diverges from that of enzymes belonging to the conventional tyrosinase family in several ways, particularly around the central α-helical core region. A diatomic oxygen moiety was identified as a bridging molecule between the two copper ions CuA and CuB separated by a distance of 4.2-4.3 Å. The UV/vis absorption spectrum of AoCO4 exhibits a distinct maximum of absorbance at 350 nm, which has been reported to be typical of the oxy form of type 3 copper enzymes.