1tzl
From Proteopedia
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Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.
Overview
Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates, using dioxygen. The enzyme forms a D(2) symmetric homotetramer and, contains one covalently bound FAD per subunit. The structure of the enzyme, from Peniophora sp. was determined by multiwavelength anomalous, diffraction (MAD) based on 96 selenium sites per crystallographic, asymmetric unit and subsequently refined to good-quality indices., According to its chain fold, the enzyme belongs to the large glutathione, reductase family and, in a more narrow sense, to the, glucose-methanol-choline oxidoreductase (GMC) family. The tetramer, contains a spacious central cavity from which the substrate enters one of, the four active centers by penetrating a mobile barrier. Since this cavity, can only be accessed by glucose-sized molecules, the enzyme does not, convert sugars that are part of a larger molecule. The geometry of the, active center and a comparison with an inhibitor complex of the homologous, enzyme cellobiose dehydrogenase allow the modeling of the reaction at a, high confidence level.
About this Structure
1TZL is a Single protein structure of sequence from Peniophora sp. sg with FAD as ligand. Active as Pyranose oxidase, with EC number 1.1.3.10 Full crystallographic information is available from OCA.
Reference
Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp., Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE, Biochemistry. 2004 Sep 21;43(37):11683-90. PMID:15362852
Page seeded by OCA on Wed Nov 21 03:43:31 2007
