5d7z

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<StructureSection load='5d7z' size='340' side='right'caption='[[5d7z]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
<StructureSection load='5d7z' size='340' side='right'caption='[[5d7z]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5d7z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ro6 4ro6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D7Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5d7z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ro6 4ro6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D7Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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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]] 1.73&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Zm.67052, ZEAMMB73_635823 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</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=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr>
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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=5d7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7z OCA], [https://pdbe.org/5d7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d7z RCSB], [https://www.ebi.ac.uk/pdbsum/5d7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7z ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7z OCA], [http://pdbe.org/5d7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d7z RCSB], [http://www.ebi.ac.uk/pdbsum/5d7z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7z ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/B6TPH0_MAIZE B6TPH0_MAIZE]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.[RuleBase:RU361179]
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[https://www.uniprot.org/uniprot/B6TPH0_MAIZE B6TPH0_MAIZE] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.[RuleBase:RU361179]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated under diverse metabolic stress conditions, such as in the defence response to infection by pathogenic microorganisms. Despite their proven fundamental role in metabolic stresses, plant glyoxalases have been poorly studied. In this work, glyoxalase I from Zea mays has been characterized both biochemically and structurally, thus reporting the first atomic model of a glyoxalase I available from plants. The results indicate that this enzyme comprises a single polypeptide with two structurally similar domains, giving rise to two lateral concavities, one of which harbours a functional nickel(II)-binding active site. The putative function of the remaining cryptic active site remains to be determined.
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Structure of the novel monomeric glyoxalase I from Zea mays.,Turra GL, Agostini RB, Fauguel CM, Presello DA, Andreo CS, Gonzalez JM, Campos-Bermudez VA Acta Crystallogr D Biol Crystallogr. 2015 Oct 1;71(Pt 10):2009-20. doi:, 10.1107/S1399004715015205. Epub 2015 Sep 26. PMID:26457425<ref>PMID:26457425</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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<div class="pdbe-citations 5d7z" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lactoylglutathione lyase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Maize]]
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[[Category: Zea mays]]
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[[Category: Gonzalez, J M]]
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[[Category: Gonzalez JM]]
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[[Category: Lyase]]
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Current revision

Crystal structure of glyoxalase I from Zea mays

PDB ID 5d7z

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