View source for 4ogg


==Crystal Structure of Arabidopsis thaliana DJ-1d with glyoxylate as substrate analog==
<StructureSection load='4ogg' size='340' side='right'caption='[[4ogg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ogg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OGG 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=CGV:S-[(R)-CARBOXY(HYDROXY)METHYL]-L-CYSTEINE'>CGV</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=4ogg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ogg OCA], [https://pdbe.org/4ogg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ogg RCSB], [https://www.ebi.ac.uk/pdbsum/4ogg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ogg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DJ1D_ARATH DJ1D_ARATH] Possesses glyoxalase I activity. Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. May be involved in oxidative stress response.<ref>PMID:23651081</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DJ-1 family proteins have recently been characterized as novel glyoxalases, although their cofactor-free catalytic mechanisms are not fully understood. In this work, we obtained crystals of Arabidopsis thaliana DJ-1d (atDJ-1d) and Homo sapiens DJ-1 (hDJ-1) covalently bound to glyoxylate, an analog of methylglyoxal, forming a hemithioacetal that presumably mimics an intermediate structure in the catalysis from methylglyoxal to lactate. The level of deuteration in lactate formation supported the proton transfer mechanism in the enzyme reaction. Differences in the enantiomeric specificity of D/L-lactacte formation observed in the DJ-1 superfamily proteins were explained by the presence of a His residue in the active site with essential Cys and Glu residues. The model for the stereospecificity was further evaluated by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The DJ-1 glyoxalase provides a unique mechanism in understanding the His residue-involved stereospecificity. This article is protected by copyright. All rights reserved.

Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures.,Choi D, Kim J, Ha S, Kwon K, Kim EH, Lee HY, Ryu KS, Park C FEBS J. 2014 Oct 4. doi: 10.1111/febs.13085. PMID:25283443<ref>PMID:25283443</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ogg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Protein DJ-1|Protein DJ-1]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Choi D]]
[[Category: Kim J]]
[[Category: Park C]]
[[Category: Ryu K-S]]