View source for 6bnz


==Crystal structure of E144Q-glyoxalase I mutant from Zea mays in space group P4(1)2(1)2==
<StructureSection load='6bnz' size='340' side='right'caption='[[6bnz]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bnz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BNZ 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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=6bnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnz OCA], [https://pdbe.org/6bnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bnz RCSB], [https://www.ebi.ac.uk/pdbsum/6bnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B6TPH0_MAIZE B6TPH0_MAIZE] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.[RuleBase:RU361179]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into d-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxalase I from maize exhibits a symmetric fold with two cavities, potentially harboring two active sites, in analogy with homodimeric enzyme surrogates. Here we confirm that only one of the two cavities exhibits glyoxalase I activity and show that it adopts a tunnel-shaped structure upon substrate binding. Such conformational change gives rise to independent binding sites for glutathione and methylglyoxal in the same active site, with important implications for the molecular reaction mechanism, which has been a matter of debate for several decades. DATABASE: Structural data are available in The Protein Data Bank database under the accession numbers 6BNN, 6BNX, and 6BNZ.

Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays.,Gonzalez JM, Agostini RB, Alvarez CE, Klinke S, Andreo CS, Campos-Bermudez VA FEBS J. 2019 Apr 16. doi: 10.1111/febs.14855. PMID:30993890<ref>PMID:30993890</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bnz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Agostini RB]]
[[Category: Alvarez CE]]
[[Category: Campos Bermudez VA]]
[[Category: Drincovich MF]]
[[Category: Gonzalez JM]]
[[Category: Klinke S]]