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

Nature Structural Biology volume 9, pages 601–605 (2002)Cite this article

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.

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Figure 1: Three-dimensional structures of a, MaL and b, CcL.
Figure 2: Molecular surfaces of a, MaL and b, CcL.
Figure 3: Copper and oxygen binding to MaL

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Acknowledgements

This work was supported by TEKES (Structural Biology Research Program), the Academy of Finland (Finnish Centre of Excellence Programme (V.T.T.)) and the Neste Foundation.

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Authors and Affiliations

  1. Department of Chemistry, University of Joensuu, PO BOX 111, Joensuu, FIN-80101, Finland

    Nina Hakulinen & Juha Rouvinen

  2. VTT Biotechnology, PO BOX 1500, Espoo, FIN-02044 VTT, Finland

    Laura-Leena Kiiskinen, Kristiina Kruus, Markku Saloheimo, Arja Paananen & Anu Koivula

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  1. Nina Hakulinen
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Hakulinen, N., Kiiskinen, LL., Kruus, K. et al. Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nat Struct Mol Biol 9, 601–605 (2002). https://doi.org/10.1038/nsb823

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