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Substrate and dioxygen binding to the endospore coat laccase CotA from Bacillus subtilisSubstrate and dioxygen binding to the endospore coat laccase CotA from Bacillus subtilis
Structural highlights
FunctionCOTA_BACSU Involved in brown pigmentation during sporogenesis. Publication Abstract from PubMedThe 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. Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.,Enguita FJ, Marcal D, Martins LO, Grenha R, Henriques AO, Lindley PF, Carrondo MA J Biol Chem. 2004 May 28;279(22):23472-6. Epub 2004 Feb 4. PMID:14764581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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