4J3Q
Crystal structure of truncated catechol oxidase from Aspergillus oryzae
Summary for 4J3Q
| Entry DOI | 10.2210/pdb4j3q/pdb |
| Related | 4J3P 4J3R |
| Descriptor | catechol oxidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (5 entities in total) |
| Functional Keywords | catechol oxidase, type-3 copper center, binuclear copper enzyme, glycosylated, oxidoreductase |
| Biological source | Aspergillus oryzae (Yellow koji mold) |
| Total number of polymer chains | 2 |
| Total formula weight | 76726.75 |
| Authors | Hakulinen, N.,Gasparetti, C.,Kaljunen, H.,Rouvinen, J. (deposition date: 2013-02-06, release date: 2013-11-27, Last modification date: 2024-10-16) |
| Primary citation | Hakulinen, N.,Gasparetti, C.,Kaljunen, H.,Kruus, K.,Rouvinen, J. The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae. J.Biol.Inorg.Chem., 18:917-929, 2013 Cited by PubMed 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. PubMed: 24043469DOI: 10.1007/s00775-013-1038-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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