title: Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.
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.
authors.affiliation: Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
authors.forename: V
authors.initials: V
authors.lastname: Ducros
authors.forename: A M
authors.initials: AM
authors.lastname: Brzozowski
authors.forename: K S
authors.initials: KS
authors.lastname: Wilson
authors.forename: P
authors.initials: P
authors.lastname: Ostergaard
authors.forename: P
authors.initials: P
authors.lastname: Schneider
authors.forename: A
authors.initials: A
authors.lastname: Svendson
authors.forename: G J
authors.initials: GJ
authors.lastname: Davies
mesh_terms: D001665:Binding Sites; D003300:Copper / Q000378:metabolism; D003302:Coprinus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D042845:Laccase; D008958:Models, Molecular; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D007527:Isoenzymes; D003300:Copper; D010088:Oxidoreductases; D042845:Laccase