BACILLUS SUBTILIS COTA LACCASE ADDUCT WITH ABTS

File:1uvw.gif


1uvw, resolution 2.45Å

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OverviewOverview

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.

About this StructureAbout this Structure

1UVW is a Single protein structure of sequence from Bacillus subtilis with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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

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