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| | <StructureSection load='5lkd' size='340' side='right'caption='[[5lkd]], [[Resolution|resolution]] 1.68Å' scene=''> | | <StructureSection load='5lkd' size='340' side='right'caption='[[5lkd]], [[Resolution|resolution]] 1.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lkd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LKD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lkd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LKD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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]] 1.68Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECM4, GTO2, YKR076W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://proteopedia.org/fgij/fg.htm?mol=5lkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkd OCA], [http://pdbe.org/5lkd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lkd RCSB], [http://www.ebi.ac.uk/pdbsum/5lkd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkd ProSAT]</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=5lkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkd OCA], [https://pdbe.org/5lkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lkd RCSB], [https://www.ebi.ac.uk/pdbsum/5lkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GTO2_YEAST GTO2_YEAST]] Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis.<ref>PMID:16709151</ref> | + | [https://www.uniprot.org/uniprot/GTO2_YEAST GTO2_YEAST] Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis.<ref>PMID:16709151</ref> |
| | <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 5lkd" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5lkd" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Didierjean, C]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Favier, F]] | + | [[Category: Didierjean C]] |
| - | [[Category: Gelhaye, E]] | + | [[Category: Favier F]] |
| - | [[Category: Girardet, J M]] | + | [[Category: Gelhaye E]] |
| - | [[Category: Hecker, A]] | + | [[Category: Girardet JM]] |
| - | [[Category: Morel-Rouhier, M]] | + | [[Category: Hecker A]] |
| - | [[Category: Schwartz, M]] | + | [[Category: Morel-Rouhier M]] |
| - | [[Category: Ecm4]]
| + | [[Category: Schwartz M]] |
| - | [[Category: Glutathione]]
| + | |
| - | [[Category: Glutathione transferase]]
| + | |
| - | [[Category: Glutathionyl-hydroquinone reductase]]
| + | |
| - | [[Category: Quinone]]
| + | |
| - | [[Category: Saccharomyces cerevisiae]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Ykr076w]]
| + | |
| Structural highlights
Function
GTO2_YEAST Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis.[1]
Publication Abstract from PubMed
Glutathionyl-hydroquinone reductases (GHRs) belong to the recently characterized Xi-class of glutathione transferases (GSTXs) according to unique structural properties and are present in all but animal kingdoms. The GHR ScECM4 from the yeast Saccharomyces cerevisiae has been studied since 1997 when it was found to be potentially involved in cell-wall biosynthesis. Up to now and in spite of biological studies made on this enzyme, its physiological role remains challenging. The work here reports its crystallographic study. In addition to exhibiting the general GSTX structural features, ScECM4 shows extensions including a huge loop which contributes to the quaternary assembly. These structural extensions are probably specific to Saccharomycetaceae. Soaking of ScECM4 crystals with GS-menadione results in a structure where glutathione forms a mixed disulfide bond with the cysteine 46. Solution studies confirm that ScECM4 has reductase activity for GS-menadione in presence of glutathione. Moreover, the high resolution structures allowed us to propose new roles of conserved residues of the active site to assist the cysteine 46 during the catalytic act.
Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.,Schwartz M, Didierjean C, Hecker A, Girardet JM, Morel-Rouhier M, Gelhaye E, Favier F PLoS One. 2016 Oct 13;11(10):e0164678. doi: 10.1371/journal.pone.0164678., eCollection 2016. PMID:27736955[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Garcera A, Barreto L, Piedrafita L, Tamarit J, Herrero E. Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases. Biochem J. 2006 Sep 1;398(2):187-96. PMID:16709151 doi:http://dx.doi.org/10.1042/BJ20060034
- ↑ Schwartz M, Didierjean C, Hecker A, Girardet JM, Morel-Rouhier M, Gelhaye E, Favier F. Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones. PLoS One. 2016 Oct 13;11(10):e0164678. doi: 10.1371/journal.pone.0164678., eCollection 2016. PMID:27736955 doi:http://dx.doi.org/10.1371/journal.pone.0164678
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