6bnx: Difference between revisions
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<StructureSection load='6bnx' size='340' side='right'caption='[[6bnx]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6bnx' size='340' side='right'caption='[[6bnx]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bnx]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6bnx]] 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=6BNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BNX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <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></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=6bnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnx OCA], [https://pdbe.org/6bnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bnx RCSB], [https://www.ebi.ac.uk/pdbsum/6bnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnx ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6bnx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6bnx" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Zea mays]] | ||
[[Category: Agostini | [[Category: Agostini RB]] | ||
[[Category: Alvarez | [[Category: Alvarez CE]] | ||
[[Category: Bermudez | [[Category: Campos Bermudez VA]] | ||
[[Category: Drincovich | [[Category: Drincovich MF]] | ||
[[Category: Gonzalez | [[Category: Gonzalez JM]] | ||
[[Category: Klinke | [[Category: Klinke S]] | ||
Latest revision as of 17:46, 4 October 2023
Crystal structure of V278E-glyoxalase I mutant from Zea mays in space group P6(3)Crystal structure of V278E-glyoxalase I mutant from Zea mays in space group P6(3)
Structural highlights
FunctionB6TPH0_MAIZE Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.[RuleBase:RU361179] Publication Abstract from PubMedDetoxification 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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