1gw0
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CRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORM
OverviewOverview
We have crystallized the ascomycete laccase from Melanocarpus albomyces, with all four coppers present and determined the crystal structure at 2.4, A resolution. The enzyme is heavily glycosylated and consists of three, cupredoxin-like domains, similar to those found in the Cu-depleted, basidiomycete laccase from Coprinus cinereus. However, there are, significant differences in the loops forming the substrate-binding pocket., In addition, the crystal structure of the M. albomyces laccase revealed, elongated electron density between all three coppers in the trinuclear, copper site, suggesting that an oxygen molecule binds with a novel, geometry. This oxygen, required in the reaction, may enter the trinuclear, site through the tunnel, which is open in the structure of the C. cinereus, laccase. In contrast, the C-terminus on the M. albomyces laccase forms a, plug that blocks this access.
About this StructureAbout this Structure
1GW0 is a Single protein structure of sequence from Melanocarpus albomyces with , , , and as ligands. Active as Laccase, with EC number 1.10.3.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site., Hakulinen N, Kiiskinen LL, Kruus K, Saloheimo M, Paananen A, Koivula A, Rouvinen J, Nat Struct Biol. 2002 Aug;9(8):601-5. PMID:12118243
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