Nature Structural Biology
5, 310 - 316 (1998)
doi:10.1038/nsb0498-310
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolutionValérie Ducros1, Andrzej Marek Brzozowski1, Keith S. Wilson1, Stephen H. Brown2, Peter Østergaard2, Palle Schneider2, Debbie S. Yaver2, Anders H Pedersen2
& Gideon J. Davies1, 3
1Department of Chemistry, University of York, Heslington, York Y01 5DD, UK.
2Novo-Nordisk a/s, Novo allé, DK-2880 Bagsvaerd, Denmark.
3email: davies@yorvic.york.ac.uk 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  -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.
|
