2ete

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{{Seed}}
 
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[[Image:2ete.png|left|200px]]
 
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==Recombinant oxalate oxidase in complex with glycolate==
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The line below this paragraph, containing "STRUCTURE_2ete", creates the "Structure Box" on the page.
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<StructureSection load='2ete' size='340' side='right'caption='[[2ete]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ete]] is a 2 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=2ETE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ETE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<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>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_2ete| PDB=2ete | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ete FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ete OCA], [https://pdbe.org/2ete PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ete RCSB], [https://www.ebi.ac.uk/pdbsum/2ete PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ete ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/et/2ete_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ete ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Recombinant oxalate oxidase in complex with glycolate===
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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<ref>PMID:16291738</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16291738}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2ete" style="background-color:#fffaf0;"></div>
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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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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16291738}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2ETE 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=2ETE OCA].
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==Reference==
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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]
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Oxalate oxidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Opaleye O]]
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[[Category: Opaleye, O.]]
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[[Category: Pickersgill RW]]
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[[Category: Pickersgill, R W.]]
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[[Category: Rose R-S]]
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[[Category: Rose, R S.]]
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[[Category: Whittaker JW]]
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[[Category: Whittaker, J W.]]
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[[Category: Whittaker MM]]
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[[Category: Whittaker, M M.]]
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[[Category: Woo E-J]]
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[[Category: Woo, E J.]]
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[[Category: Cupin]]
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[[Category: Double stranded beta-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:25:33 2008''
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Current revision

Recombinant oxalate oxidase in complex with glycolate

PDB ID 2ete

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OCA

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