6ZIJ

Crystal Structure of Two-Domain Laccase mutant R240H from Streptomyces griseoflavus

6ZIJ の概要

• エントリーDOI: 10.2210/pdb6zij/pdb
• 分子名称: Two-domain laccase, COPPER (II) ION, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: two-domain laccase, laccase, streptomyces griseoflavus, oxidoreductase
• 由来する生物種: Streptomyces griseoflavus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 210770.16

構造登録者

Gabdulkhakov, A.G.,Tishchenko, T.V.,Kolyadenko, I.A. (登録日: 2020-06-26, 公開日: 2021-05-05, 最終更新日: 2024-01-31)

主引用文献

Gabdulkhakov, A.,Kolyadenko, I.,Oliveira, P.,Tamagnini, P.,Mikhaylina, A.,Tishchenko, S.
The role of positive charged residue in the proton-transfer mechanism of two-domain laccase from Streptomyces griseoflavus Ac-993.
J.Biomol.Struct.Dyn., 40:8324-8331, 2022

PubMed Abstract: Multi-copper oxidases are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. This process takes place at the trinuclear copper center of the enzymes. Previously, the main catalytic stages for three-domain (3D) laccases have been identified. However, for bacterial small two-domain (2D) laccases several questions remain to be answered. One of them is the nature of the protonation events upon the reductive cleavage of dioxygen to water. In 3D laccases, acidic residues play a key role in the protonation mechanisms. In this study, the role of the Arg240 residue, located within the T2 tunnel of 2D laccase from Ac-993, was investigated. X-ray structural analysis and kinetic characterization of two mutants, R240A and R240H, have provided support for a role of this residue in the protonation events. Communicated by Ramaswamy H. Sarma.

PubMed: 33870857
DOI: 10.1080/07391102.2021.1911852

実験手法

X-RAY DIFFRACTION (1.6 Å)