2ete
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(New page: 200px<br /><applet load="2ete" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ete, resolution 1.75Å" /> '''Recombinant oxalate ...)
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Revision as of 08:00, 21 November 2007
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Recombinant oxalate oxidase in complex with glycolate
Overview
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.
About this Structure
2ETE is a Single protein structure of sequence from Hordeum vulgare with NAG, MN and GLV as ligands. Active as Oxalate oxidase, with EC number 1.2.3.4 Full crystallographic information is available from OCA.
Reference
Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase., Opaleye O, Rose RS, Whittaker MM, Woo EJ, Whittaker JW, Pickersgill RW, J Biol Chem. 2006 Mar 10;281(10):6428-33. Epub 2005 Nov 15. PMID:16291738
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