2ete
From Proteopedia
(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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| - | [[Image:2ete.gif|left|200px]]<br /><applet load="2ete" size=" | + | [[Image:2ete.gif|left|200px]]<br /><applet load="2ete" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ete, resolution 1.75Å" /> | caption="2ete, resolution 1.75Å" /> | ||
'''Recombinant oxalate oxidase in complex with glycolate'''<br /> | '''Recombinant oxalate oxidase in complex with glycolate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Oxalate oxidase (EC 1.2.3.4) catalyzes the conversion of oxalate and | + | 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== | ==About this Structure== | ||
| - | 2ETE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with NAG, MN and GLV as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2ETE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=GLV:'>GLV</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ETE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Opaleye, O.]] | [[Category: Opaleye, O.]] | ||
| - | [[Category: Pickersgill, R | + | [[Category: Pickersgill, R W.]] |
| - | [[Category: Rose, R | + | [[Category: Rose, R S.]] |
| - | [[Category: Whittaker, J | + | [[Category: Whittaker, J W.]] |
| - | [[Category: Whittaker, M | + | [[Category: Whittaker, M M.]] |
| - | [[Category: Woo, E | + | [[Category: Woo, E J.]] |
[[Category: GLV]] | [[Category: GLV]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: double stranded beta-helix]] | [[Category: double stranded beta-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:29 2008'' |
Revision as of 15:14, 21 February 2008
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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 , and 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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