2ete

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[[Image:2ete.gif|left|200px]]
[[Image:2ete.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2ete |SIZE=350|CAPTION= <scene name='initialview01'>2ete</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_2ete", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2ete| PDB=2ete | SCENE= }}
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|RELATEDENTRY=[[1fi2|1fi2]], [[2et1|2et1]], [[2et7|2et7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ete FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ete OCA], [http://www.ebi.ac.uk/pdbsum/2ete PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ete RCSB]</span>
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}}
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'''Recombinant oxalate oxidase in complex with glycolate'''
'''Recombinant oxalate oxidase in complex with glycolate'''
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[[Category: Whittaker, M M.]]
[[Category: Whittaker, M M.]]
[[Category: Woo, E J.]]
[[Category: Woo, E J.]]
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[[Category: cupin]]
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[[Category: Cupin]]
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[[Category: double stranded beta-helix]]
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[[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 Mon Mar 31 02:53:33 2008''
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Revision as of 00:05, 4 May 2008

Image:2ete.gif

Template:STRUCTURE 2ete

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. 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 Sun May 4 03:05:45 2008

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