5o4q
Crystal Structure of mutant M54L/M64L/M96L of Two-Domain Laccase from Streptomyces griseoflavus with 0.25 mM copper sulfate on growth mediumCrystal Structure of mutant M54L/M64L/M96L of Two-Domain Laccase from Streptomyces griseoflavus with 0.25 mM copper sulfate on growth medium
Structural highlights
FunctionPublication Abstract from PubMedLaccase 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. [Incorporation of Copper Ions into T2/T3 Centers of Two-Domain Laccases].,Gabdulkhakov AG, Kostareva OS, Kolyadenko IA, Mikhaylina AO, Trubitsina LI, Tishchenko SV Mol Biol (Mosk). 2018 Jan-Feb;52(1):29-35. doi: 10.7868/S0026898418010056. PMID:29512633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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