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Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site
- Source :
- Hakulinen, N, Kiiskinen, L-L, Kruus, K, Saloheimo, M, Paananen, A, Koivula, A & Rouvinen, J 2002, ' Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site ', Nature Structural Biology, vol. 9, no. 8, pp. 601-605 . https://doi.org/10.1038/nsb823
- Publication Year :
- 2002
- Publisher :
- Nature Publishing Group, 2002.
-
Abstract
- We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 Å 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.
- Subjects :
- Models, Molecular
crystal structure
Stereochemistry
Protein Conformation
Molecular Sequence Data
Static Electricity
Sordariales
chemistry.chemical_element
Crystal structure
Crystallography, X-Ray
Biochemistry
laccase
Melanocarpus albomyces laccase
Coprinus
Species Specificity
Structural Biology
Oxidoreductase
Catalytic Domain
Genetics
Molecule
Amino Acid Sequence
chemistry.chemical_classification
Laccase
Binding Sites
Sequence Homology, Amino Acid
Copper
Oxygen
Enzyme
chemistry
Melanocarpus albomyces
Coprinus cinereus
Oxidoreductases
Subjects
Details
- Language :
- English
- ISSN :
- 15459985 and 15459993
- Volume :
- 9
- Issue :
- 8
- Database :
- OpenAIRE
- Journal :
- Nature Structural and Molecular Biology
- Accession number :
- edsair.doi.dedup.....4bfc2577fa351032b237065fa28f1fe2