Feb 7, 2004

Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis

The Journal of Biological Chemistry
Francisco J EnguitaM Arménia Carrondo


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.

  • References19
  • Citations68


  • References19
  • Citations68


Mentioned in this Paper

Laccase B
Plasma Protein Binding Capacity
Cota <angiosperm>
Ligand Binding Domain
Bacillus subtilis
Substrate Specificity
Protein Conformation
Mediator of activation protein

Related Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.