1j58

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spinqualitylabelsall models 1j58, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Oxalate Decarboxylase

Overview

Oxalate decarboxylase is a manganese-dependent enzyme that catalyzes the, conversion of oxalate to formate and carbon dioxide. We have determined, the structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A, resolution in the presence of formate. The structure reveals a hexamer, with 32-point symmetry in which each monomer belongs to the cupin family, of proteins. Oxalate decarboxylase is further classified as a bicupin, because it contains two cupin folds, possibly resulting from gene, duplication. Each oxalate decarboxylase cupin domain contains one, manganese binding site. Each of the oxalate decarboxylase domains is, structurally similar to oxalate oxidase, which catalyzes the, manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide, and hydrogen peroxide. Amino acid side chains in the two metal binding, sites of oxalate decarboxylase and the metal binding site of oxalate, oxidase are very similar. Four manganese binding residues (three, histidines and one glutamate) are conserved as well as a number of, hydrophobic residues. The most notable difference is the presence of, Glu333 in the metal binding site of the second cupin domain of oxalate, decarboxylase. We postulate that this domain is responsible for the, decarboxylase activity and that Glu333 serves as a proton donor in the, production of formate. Mutation of Glu333 to alanine reduces the catalytic, activity by a factor of 25. The function of the other domain in oxalate, decarboxylase is not yet known.

About this Structure

1J58 is a Single protein structure of sequence from Bacillus subtilis with MN, MG and FMT as ligands. Full crystallographic information is available from OCA.

Reference

Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution., Anand R, Dorrestein PC, Kinsland C, Begley TP, Ealick SE, Biochemistry. 2002 Jun 18;41(24):7659-69. PMID:12056897

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