1gyc
CRYSTAL STRUCTURE DETERMINATION AT ROOM TEMPERATURE OF A LACCASE FROM TRAMETES VERSICOLOR IN ITS OXIDISED FORM CONTAINING A FULL COMPLEMENT OF COPPER IONS
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OverviewOverview
Laccase is a polyphenol oxidase, which belongs to the family of blue, multicopper oxidases. These enzymes catalyze the one-electron oxidation of, four reducing-substrate molecules concomitant with the four-electron, reduction of molecular oxygen to water. Laccases oxidize a broad range of, substrates, preferably phenolic compounds. In the presence of mediators, fungal laccases exhibit an enlarged substrate range and are then able to, oxidize compounds with a redox potential exceeding their own. Until now, only one crystal structure of a laccase in an inactive, type-2, copper-depleted form has been reported. We present here the first crystal, structure of an active laccase containing a full complement of coppers, the complete polypeptide chain together with seven carbohydrate moieties., ... [(full description)]
About this StructureAbout this Structure
1GYC is a [Single protein] structure of sequence from [Trametes versicolor] with NAG, CU and IPA as [ligands]. Active as [Laccase], with EC number [1.10.3.2]. Structure known Active Site: CU1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers., Piontek K, Antorini M, Choinowski T, J Biol Chem. 2002 Oct 4;277(40):37663-9. Epub 2002 Aug 5. PMID:12163489
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