title: Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.
abstract: The CotA laccase from the endospore coat of Bacillus subtilis has been crystallized in the presence of the non-catalytic co-oxidant 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS), and the structure was determined using synchrotron radiation. The binding site for this adduct is well defined and indicates how ABTS, in conjunction with laccases, could act as an oxidative mediator toward non-phenolic moieties. In addition, a dioxygen moiety is clearly defined within the solvent channel oriented toward one of the T3 copper atoms in the trinuclear center.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal.
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Enguita
authors.forename: David
authors.initials: D
authors.lastname: Marçal
authors.forename: Lígia O
authors.initials: LO
authors.lastname: Martins
authors.forename: Rosa
authors.initials: R
authors.lastname: Grenha
authors.forename: Adriano O
authors.initials: AO
authors.lastname: Henriques
authors.forename: Peter F
authors.initials: PF
authors.lastname: Lindley
authors.forename: Maria Arménia
authors.initials: MA
authors.lastname: Carrondo
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D001665:Binding Sites; D042845:Laccase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010100:Oxygen / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D042845:Laccase; D010100:Oxygen