2et7
From Proteopedia
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| - | [[Image:2et7.gif|left|200px]] | + | [[Image:2et7.gif|left|200px]] |
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| - | '''Structural and spectroscopic insights into the mechanism of oxalate oxidase''' | + | {{Structure |
| + | |PDB= 2et7 |SIZE=350|CAPTION= <scene name='initialview01'>2et7</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Oxalate_oxidase Oxalate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.4 1.2.3.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structural and spectroscopic insights into the mechanism of oxalate oxidase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ET7 is a [ | + | 2ET7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ET7 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16291738 16291738] |
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Oxalate oxidase]] | [[Category: Oxalate oxidase]] | ||
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[[Category: double stranded beta-helix]] | [[Category: double stranded beta-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:44:07 2008'' |
Revision as of 14:44, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | |||||||
| Activity: | Oxalate oxidase, with EC number 1.2.3.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural and spectroscopic insights into the mechanism of oxalate oxidase
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
2ET7 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
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