1gw0
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We have crystallized the ascomycete laccase from Melanocarpus albomyces | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hakulinen, N.]] | [[Category: Hakulinen, N.]] | ||
| - | [[Category: Kiiskinen, L | + | [[Category: Kiiskinen, L L.]] |
[[Category: Koivula, A.]] | [[Category: Koivula, A.]] | ||
[[Category: Kruus, K.]] | [[Category: Kruus, K.]] | ||
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[[Category: oxygen reduction]] | [[Category: oxygen reduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:34 2008'' |
Revision as of 10:54, 21 February 2008
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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 laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.
About 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.
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 Thu Feb 21 12:54:34 2008
Categories: Laccase | 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 | Multi-copper oxidases | Oxygen reduction
