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

Nat Struct Biol. 1998 Apr;5(4):310-6. doi: 10.1038/nsb0498-310.


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 A. Laccase is a monomer composed of three cupredoxin-like beta-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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Ascorbate Oxidase / chemistry
  • Azurin / analogs & derivatives
  • Azurin / chemistry
  • Binding Sites
  • Copper
  • Coprinus / enzymology*
  • Crystallography, X-Ray / methods
  • Humans
  • Laccase
  • Molecular Sequence Data
  • Oxidoreductases / chemistry*
  • Protein Conformation*
  • Protein Structure, Secondary*
  • Recombinant Proteins / chemistry


  • Recombinant Proteins
  • cupredoxin
  • Azurin
  • Copper
  • Oxidoreductases
  • Laccase
  • Ascorbate Oxidase

Associated data

  • PDB/1A65