1gw0
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(New page: 200px<br /> <applet load="1gw0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gw0, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:13, 29 October 2007
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CRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORM
Overview
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, ... [(full description)]
About this Structure
1GW0 is a [Single protein] structure of sequence from [Melanocarpus albomyces] with NAG, CU, CL, SO4 and OXY as [ligands]. Active as [[1]], with EC number [1.10.3.2]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 16:17:59 2007
Categories: Melanocarpus albomyces | Single protein | Hakulinen, N. | Kiiskinen, L.L. | Koivula, A. | Kruus, K. | Rouvinen, J. | Saloheimo, M. | CL | CU | NAG | OXY | SO4 | Ascomycete | C-terminal plug | Laccase | Multi-copper oxidases | Oxygen reduction