Structure of the laccase from Coprinus cinereus at 1.68 angstrom resolution: evidence for different 'type 2 Cu-depleted ' isoforms

V Ducros, A M Brzozowski, K S Wilson, P Ostergaard, P Schneider, A Svendson, G J Davies

Research output: Contribution to journalArticlepeer-review

Abstract

Laccases (E.C. 1.10.3.2; benzenediol oxygen oxidoreductases) couple the four-electron reduction of dioxygen to water to four one-electron oxidations of a reducing substrate. The three-dimensional structure of the 'blue' multi-copper oxidase laccase from the fungus Coprinus cinereus at 1.68 Angstrom reveals the structural basis for isoforms of the type 2 Cu-depleted species.

Original languageEnglish
Pages (from-to)333-336
Number of pages4
JournalActa Crystallographica. Section D, Biological Crystallography
Volume57
Publication statusPublished - Feb 2001

Keywords

  • PHOTOREALISTIC MOLECULAR GRAPHICS
  • FUNGAL LACCASES
  • PROTEIN STRUCTURES
  • CRYSTAL-STRUCTURE
  • DEPLETED LACCASE
  • RHUS LACCASE
  • TYPE-3 SITE
  • COPPER SITE
  • OXIDATION
  • OXIDASE

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