3ZDW

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

Replaces:  1UVW

Summary for 3ZDW

• Entry DOI: 10.2210/pdb3zdw/pdb
• Descriptor: COTA LACCASE, COPPER (I) ION, OXYGEN MOLECULE, ... (6 entities in total)
• Functional Keywords: hydrolase, abts
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 60020.25

Authors

Enguita, F.J.,Marcal, D.,Grenha, R.,Lindley, P.F.,Carrondo, M.A. (deposition date: 2012-12-01, release date: 2012-12-19, Last modification date: 2024-10-16)

Primary citation

Enguita, F.J.,Marcal, D.,Martins, L.O.,Grenha, R.,Henriques, A.O.,Lindley, P.F.,Carrondo, M.A.
Substrate and Dioxygen Binding to the Endospore Coat Laccase from Bacillus Subtilis.
J.Biol.Chem., 279:23472-, 2004

PubMed 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.

PubMed: 14764581
DOI: 10.1074/JBC.M314000200

Experimental method

X-RAY DIFFRACTION (2.4 Å)