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| | ==Crystal structure of glyoxalase III (Orf 19.251) from Candida albicans== | | ==Crystal structure of glyoxalase III (Orf 19.251) from Candida albicans== |
| - | <StructureSection load='4lru' size='340' side='right' caption='[[4lru]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4lru' size='340' side='right'caption='[[4lru]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lru]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canal Canal]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LRU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lru]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LRU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.7882, Orf 19.251, orf19.7882 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 CANAL])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-lactate_dehydratase D-lactate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.130 4.2.1.130] </span></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=4lru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lru OCA], [https://pdbe.org/4lru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lru RCSB], [https://www.ebi.ac.uk/pdbsum/4lru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lru ProSAT]</span></td></tr> |
| - | <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=4lru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lru OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lru RCSB], [http://www.ebi.ac.uk/pdbsum/4lru PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HSP31_CANAL HSP31_CANAL] Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. Selective for MG, does not use glyoxal as substrate. Plays a role in detoxifying endogenously produced MG, particularly when glycerol is the principal carbon source (PubMed:24302734). Important for viability in stationary phase (By similarity).[UniProtKB:Q04432]<ref>PMID:24302734</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4lru" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Glyoxalase|Glyoxalase]] | + | *[[Glyoxalase 3D structures|Glyoxalase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Canal]] | + | [[Category: Candida albicans SC5314]] |
| - | [[Category: D-lactate dehydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Hasim, S]] | + | [[Category: Hasim S]] |
| - | [[Category: Hussin, N A]] | + | [[Category: Hussin NA]] |
| - | [[Category: Nickerson, K W]] | + | [[Category: Nickerson KW]] |
| - | [[Category: Wilson, M A]] | + | [[Category: Wilson MA]] |
| - | [[Category: Dj-1 superfamily]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
HSP31_CANAL Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. Selective for MG, does not use glyoxal as substrate. Plays a role in detoxifying endogenously produced MG, particularly when glycerol is the principal carbon source (PubMed:24302734). Important for viability in stationary phase (By similarity).[UniProtKB:Q04432][1]
Publication Abstract from PubMed
Methylglyoxal is a cytotoxic reactive carbonyl compound produced by central metabolism. Dedicated glyoxalases convert methylglyoxal to D-lactate using multiple catalytic strategies. In this study, the DJ-1 superfamily member orf 19.251/GLX3 from Candida albicans is shown to possess glyoxalase activity, making this the first demonstrated glutathione-independent glyoxalase in fungi. The crystal structure of Glx3p indicates that the protein is a monomer containing the catalytic triad Cys136-His137-Glu168. Purified Glx3p has an in vitro methylglyoxalase activity (Km = 5.5 mM and kcat = 7.8 s-1) that is significantly greater than that of more distantly related members of the DJ-1 superfamily. A close Glx3p homolog from Saccharomyces cerevisiae (YDR533C/Hsp31) also has glyoxalase activity, suggesting that fungal members of the Hsp31 clade of the DJ-1 superfamily are all probable glutathione-independent glyoxalases. A homozygous glx3 null mutant in C. albicans strain SC5314 displays greater sensitivity to millimolar levels of exogenous methylglyoxal, elevated levels of intracellular methylglyoxal, and carbon source-dependent growth defects, especially when grown on glycerol. These phenotypic defects are complemented by restoration of the wild-type GLX3 locus. The growth defect of Glx3-deficient cells in glycerol is also partially complemented by added inorganic phosphate, which is not observed for wild-type or glucose-grown cells. Therefore, C. albicans Glx3 and its fungal homologs are physiologically relevant glutathione-independent glyoxalases that are not redundant with the previously characterized glutathione-dependent GLO1/GLO2 system. In addition to its role in detoxifying glyoxals, Glx3 and its close homologs may have other important roles in stress response.
A Glutathione-Independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans.,Hasim S, Hussin NA, Alomar F, Bidasee KR, Nickerson KW, Wilson MA J Biol Chem. 2013 Dec 3. PMID:24302734[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hasim S, Hussin NA, Alomar F, Bidasee KR, Nickerson KW, Wilson MA. A Glutathione-Independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans. J Biol Chem. 2013 Dec 3. PMID:24302734 doi:http://dx.doi.org/10.1074/jbc.M113.505784
- ↑ Hasim S, Hussin NA, Alomar F, Bidasee KR, Nickerson KW, Wilson MA. A Glutathione-Independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans. J Biol Chem. 2013 Dec 3. PMID:24302734 doi:http://dx.doi.org/10.1074/jbc.M113.505784
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