Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site

Nina Hakulinen, Laura-Leena Kiiskinen, Kristiina Kruus, Markku Saloheimo, Arja Paananen, Anu Koivula, Juha Rouvinen (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    306 Citations (Scopus)

    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.
    Original languageEnglish
    Pages (from-to)601-605
    JournalNature Structural Biology
    Volume9
    Issue number8
    DOIs
    Publication statusPublished - 2002
    MoE publication typeA1 Journal article-refereed

    Keywords

    • laccase
    • Melanocarpus albomyces laccase
    • crystal structure
    • Melanocarpus albomyces

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