1GW0

Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form

Summary for 1GW0

• Entry DOI: 10.2210/pdb1gw0/pdb
• Descriptor: LACCASE-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (12 entities in total)
• Functional Keywords: oxidoreductase, laccase, multi-copper oxidases, oxygen reduction, ascomycete, c-terminal plug
• Biological source: MELANOCARPUS ALBOMYCES
• Total number of polymer chains: 2
• Total formula weight: 132160.26

Authors

Hakulinen, N.,Kiiskinen, L.-L.,Kruus, K.,Saloheimo, M.,Koivula, A.,Rouvinen, J. (deposition date: 2002-03-01, release date: 2002-07-31, Last modification date: 2024-11-13)

Primary citation

Hakulinen, N.,Kiiskinen, L.-L.,Kruus, K.,Saloheimo, M.,Paananen, A.,Koivula, A.,Rouvinen, J.
Crystal Structure of a Laccase from Melanocarpus Albomyces with an Intact Trinuclear Copper Site
Nat.Struct.Biol., 9:601-605, 2002

PubMed Abstract: 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.

PubMed: 12118243
DOI: 10.1038/NSB823

Experimental method

X-RAY DIFFRACTION (2.4 Å)