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| | <StructureSection load='2et1' size='340' side='right'caption='[[2et1]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='2et1' size='340' side='right'caption='[[2et1]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2et1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ET1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ET1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2et1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ET1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ET1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fi2|1fi2]], [[2et7|2et7]], [[2ete|2ete]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxalate_oxidase Oxalate oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.4 1.2.3.4] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2et1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2et1 OCA], [https://pdbe.org/2et1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2et1 RCSB], [https://www.ebi.ac.uk/pdbsum/2et1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2et1 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2et1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2et1 OCA], [https://pdbe.org/2et1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2et1 RCSB], [https://www.ebi.ac.uk/pdbsum/2et1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2et1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/OXO1_HORVU OXO1_HORVU]] Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms.
| + | [https://www.uniprot.org/uniprot/OXO1_HORVU OXO1_HORVU] Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Barley]] | + | [[Category: Hordeum vulgare]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oxalate oxidase]]
| + | [[Category: Opaleye O]] |
| - | [[Category: Opaleye, O]] | + | [[Category: Pickersgill RW]] |
| - | [[Category: Pickersgill, R W]] | + | [[Category: Rose R-S]] |
| - | [[Category: Rose, R S]] | + | [[Category: Woo E-J]] |
| - | [[Category: Woo, E J]] | + | |
| - | [[Category: Cupin]]
| + | |
| - | [[Category: Double stranded beta helix]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
OXO1_HORVU Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Opaleye O, Rose RS, Whittaker MM, Woo EJ, Whittaker JW, Pickersgill RW. Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase. J Biol Chem. 2006 Mar 10;281(10):6428-33. Epub 2005 Nov 15. PMID:16291738 doi:10.1074/jbc.M510256200
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