4J3R

Crystal structure of catechol oxidase from Aspergillus oryzae, soaked in 4-tert-butylcatechol

4J3R の概要

• エントリーDOI: 10.2210/pdb4j3r/pdb
• 関連するPDBエントリー: 4J3P 4J3Q
• 分子名称: catechol oxidase, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (8 entities in total)
• 機能のキーワード: catechol oxidase, type-3 copper center, binuclear copper enzyme, glycosylated, oxidoreductase
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43710.33

構造登録者

Hakulinen, N.,Gasparetti, C.,Kaljunen, H.,Rouvinen, J. (登録日: 2013-02-06, 公開日: 2013-11-27, 最終更新日: 2024-10-09)

主引用文献

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

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: 24043469
DOI: 10.1007/s00775-013-1038-9

実験手法

X-RAY DIFFRACTION (2.2 Å)