6ZIP

Crystal Structure of Two-Domain Laccase mutant R240A from Streptomyces griseoflavus

Summary for 6ZIP

• Entry DOI: 10.2210/pdb6zip/pdb
• Related: 6ZIJ
• Descriptor: Two-domain laccase, COPPER (II) ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: two-domain laccase, laccase, streptomyces griseoflavus, oxidoreductase
• Biological source: Streptomyces griseoflavus
• Total number of polymer chains: 12
• Total formula weight: 419440.76

Authors

Gabdulkhakov, A.G.,Tishchenko, T.V.,Kolyadenko, I.A. (deposition date: 2020-06-26, release date: 2021-05-05, Last modification date: 2024-01-31)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.05 Å)