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

V Ducros, A M Brzozowski, K S Wilson, S H Brown, P Ostergaard, P Schneider, D S Yaver, A H Pedersen, G J Davies

Research output: Contribution to journalArticlepeer-review

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 Angstrom. 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.

Original languageEnglish
Pages (from-to)310-316
Number of pages7
JournalNature Structural Biology
Volume5
Issue number4
Publication statusPublished - Apr 1998

Keywords

  • RHUS-VERNICIFERA LACCASE
  • COPPER ACTIVE-SITE
  • FUNGAL LACCASES
  • SPECTROSCOPIC PROPERTIES
  • ELECTRONIC-STRUCTURE
  • PROTEIN STRUCTURES
  • ASCORBATE OXIDASE
  • REFINEMENT
  • OXIDATION
  • REDUCTION

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