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Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolution

Nature Structural Biology volume 5, pages 310–316 (1998)Cite this article

Abstract

Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 Å. Laccase is a monomer composed of three cupredoxin-like β-sandwich domains, similar to that found in ascorbate oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1 Cu site lacks the axial methionine ligand and so exhibits trigonal planar coordination, consistent with its elevated redox potential. Crucially, the structure is trapped in a Cu depleted form in which the putative type-2 Cu atom is completely absent, but in which the remaining type-1 and type-3 Cu sites display full occupancy. Type-2 Cu depletion has unexpected consequences for the coordination of the remaining type-3 Cu atoms.

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Authors and Affiliations

  1. Department of Chemistry, University of York, Heslington, York, Y01 5DD, UK

    Valérie Ducros, Andrzej Marek Brzozowski, Keith S. Wilson & Gideon J. Davies

  2. Novo-Nordisk a/s, Novo allé, DK-2880, Bagsvaerd, Denmark

    Stephen H. Brown, Peter Østergaard, Palle Schneider, Debbie S. Yaver & Anders H Pedersen

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  1. Valérie Ducros
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Correspondence to Gideon J. Davies.

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Ducros, V., Brzozowski, A., Wilson, K. et al. Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolution. Nat Struct Mol Biol 5, 310–316 (1998). https://doi.org/10.1038/nsb0498-310

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