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

Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):333-6. doi: 10.1107/s0907444900013779.

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 A reveals the structural basis for isoforms of the type 2 Cu-depleted species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Copper / metabolism
  • Coprinus / enzymology*
  • Crystallization
  • Crystallography, X-Ray / methods
  • Isoenzymes / chemistry
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism
  • Laccase
  • Models, Molecular
  • Oxidoreductases / chemistry*
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism
  • Protein Conformation
  • Protein Structure, Secondary

Substances

  • Isoenzymes
  • Copper
  • Oxidoreductases
  • Laccase

Associated data

  • PDB/1A65
  • PDB/1HFU