Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site
| Autor: | Laura-Leena Kiiskinen, Markku Saloheimo, Anu Koivula, Kristiina Kruus, Nina Hakulinen, Arja Paananen, Juha Rouvinen |
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| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
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 |
| Zdroj: | 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 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsb823 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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