2et1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:57, 30 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2et1.png|left|200px]]
 
-
{{STRUCTURE_2et1| PDB=2et1 | SCENE= }}
+
==Oxalate oxidase in complex with substrate analogue glycolate==
 +
<StructureSection load='2et1' size='340' side='right'caption='[[2et1]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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='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>
 +
== 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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/et/2et1_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=2et1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===Oxalate oxidase in complex with substrate analogue glycolate===
+
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>
-
{{ABSTRACT_PUBMED_16291738}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2et1" style="background-color:#fffaf0;"></div>
-
[[2et1]] is a 1 chain structure with 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=2ET1 OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:016291738</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
-
[[Category: Oxalate oxidase]]
+
[[Category: Large Structures]]
-
[[Category: Opaleye, O.]]
+
[[Category: Opaleye O]]
-
[[Category: Pickersgill, R W.]]
+
[[Category: Pickersgill RW]]
-
[[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]]
+

Current revision

Oxalate oxidase in complex with substrate analogue glycolate

PDB ID 2et1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2et1"
Personal tools