Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus

Fusetti, F., Schröter, K. H., Steiner, R. A., Noort, P. I. V., Pijning, T., Rozeboom, H. J., Kalk, K. H., Egmond, M. R. & Dijkstra, B. W., Feb-2002, In : Structure. 10, 2, p. 259-268 10 p.

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Quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols. Dioxygenation catalyzed by iron-containing enzymes has been studied extensively, but dioxygenases employing other metal cofactors are poorly understood. We determined the crystal structure of quercetin 2,3-dioxygenase at 1.6 Angstrom resolution. The enzyme forms homodimers, which are stabilized by an N-linked heptasaccharide at the dimer interface. The mononuclear type 2 copper center displays two distinct geometries: a distorted tetrahedral coordination, formed by His66, His68, His112, and a water molecule, and a distorted trigonal bipyramidal environment, which additionally comprises Glu73. Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance.

Original languageEnglish
Pages (from-to)259-268
Number of pages10
Issue number2
Publication statusPublished - Feb-2002


  • dioxygenase, copper, cupin, glycoprotein, X-ray structure, quercetin, SEED STORAGE PROTEINS, ANGSTROM RESOLUTION, DIFFRACTION DATA, X-RAYS, DIOXYGENASE, FLAVONOL, MODELS, BOND

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