5O4I

Crystal Structure of mutant M54L/M64L/M96L of Two-Domain Laccase from Streptomyces griseoflavus dialyzed against solution containing 0.25 mM copper sulfate

Summary for 5O4I

• Entry DOI: 10.2210/pdb5o4i/pdb
• Descriptor: Two-domain laccase, COPPER (II) ION, GLYCEROL, ... (5 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: 423002.23

Authors

Gabdulkhakov, A.G.,Tishchenko, T.V. (deposition date: 2017-05-29, release date: 2018-03-28, Last modification date: 2024-01-17)

Primary citation

Gabdulkhakov, A.G.,Kostareva, O.S.,Kolyadenko, I.A.,Mikhaylina, A.O.,Trubitsina, L.I.,Tishchenko, S.V.
Incorporation of Copper Ions into T2/T3 Centers of Two-Domain Laccases.
Mol.Biol.(Moscow), 52:29-35, 2018

PubMed Abstract: Laccase belongs to the family of copper-containing oxidases. A study was made of the mechanism that sustains the incorporation of copper ions into the T2/T3 centers of recombinant two-domain laccase Streptomyces griseoflavus Ac-993. The occupancy of the T3 center by copper ions was found to increase with an increasing copper content in the culture medium and after dialysis of the protein preparation against a copper sulfate-containing buffer. The T2 center was filled only when overproducer strain cells were grown at a higher copper concentration in the medium. Two-domain laccases were assumed to possess a channel that serves to deliver copper ions to the T3 center during the formation of the three-dimensional laccase conformation and dialysis of the protein preparation. A narrower channel leads to the T2 center in two-domain laccases compared with three-domain ones, rendering the center less accessible for copper atoms. The incorporation of copper ions into the T2 center of two-domain laccases is likely to occur in the course of their biosynthesis or the formation of a functional trimer.

PubMed: 29512633
DOI: 10.7868/S0026898418010056

Experimental method

X-RAY DIFFRACTION (1.8 Å)