2ET1

Oxalate oxidase in complex with substrate analogue glycolate

Summary for 2ET1

• Entry DOI: 10.2210/pdb2et1/pdb
• Related: 1fi2 2ET7 2ETE
• Descriptor: Oxalate oxidase 1, MANGANESE (II) ION, GLYOXYLIC ACID, ... (4 entities in total)
• Functional Keywords: double stranded beta helix, cupin, oxidoreductase
• Biological source: Hordeum vulgare
• Cellular location: Secreted, extracellular space, apoplast : P45850
• Total number of polymer chains: 1
• Total formula weight: 21366.14

Authors

Rose, R.-S.,Opaleye, O.,Woo, E.-J.,Pickersgill, R.W. (deposition date: 2005-10-27, release date: 2005-11-22, Last modification date: 2024-10-30)

Primary citation

Opaleye, O.,Rose, R.-S.,Whittaker, M.M.,Woo, E.-J.,Whittaker, J.W.,Pickersgill, R.W.
Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase
J.Biol.Chem., 281:6428-6433, 2006

PubMed Abstract: Oxalate oxidase (EC 1.2.3.4) catalyzes the conversion of oxalate and dioxygen to hydrogen peroxide and carbon dioxide. In this study, glycolate was used as a structural analogue of oxalate to investigate substrate binding in the crystalline enzyme. The observed monodentate binding of glycolate to the active site manganese ion of oxalate oxidase is consistent with a mechanism involving C-C bond cleavage driven by superoxide anion attack on a monodentate coordinated substrate. In this mechanism, the metal serves two functions: to organize the substrates (oxalate and dioxygen) and to transiently reduce dioxygen. The observed structure further implies important roles for specific active site residues (two asparagines and one glutamine) in correctly orientating the substrates and reaction intermediates for catalysis. Combined spectroscopic, biochemical, and structural analyses of mutants confirms the importance of the asparagine residues in organizing a functional active site complex.

PubMed: 16291738
DOI: 10.1074/jbc.M510256200

Experimental method

X-RAY DIFFRACTION (1.6 Å)