2ete

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[[Image:2ete.gif|left|200px]]
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{{STRUCTURE_2ete| PDB=2ete | SCENE= }}
{{STRUCTURE_2ete| PDB=2ete | SCENE= }}
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'''Recombinant oxalate oxidase in complex with glycolate'''
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===Recombinant oxalate oxidase in complex with glycolate===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16291738 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16291738}}
==About this Structure==
==About this Structure==
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[[Category: Cupin]]
[[Category: Cupin]]
[[Category: Double stranded beta-helix]]
[[Category: Double stranded beta-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:05:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:25:33 2008''

Revision as of 23:25, 28 July 2008

Image:2ete.png

Template:STRUCTURE 2ete

Recombinant oxalate oxidase in complex with glycolate

Template:ABSTRACT PUBMED 16291738

About this Structure

2ETE is a Single protein structure of sequence from Hordeum vulgare. 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

Page seeded by OCA on Tue Jul 29 02:25:33 2008

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