5lkb

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae

Structural highlights

5lkb is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.45Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lkb"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae==
-<StructureSection load='5lkb' size='340' side='right' caption='[[5lkb]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+<StructureSection load='5lkb' size='340' side='right'caption='[[5lkb]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lkb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LKB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lkb]] 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=5LKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LKB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.45&#8491;</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=5lkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkb OCA], [http://pdbe.org/5lkb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lkb RCSB], [http://www.ebi.ac.uk/pdbsum/5lkb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkb ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5lkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkb OCA], [https://pdbe.org/5lkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lkb RCSB], [https://www.ebi.ac.uk/pdbsum/5lkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkb ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5lkb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Didierjean, C]]
+[[Category: Large Structures]]
-[[Category: Favier, F]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Gelhaye, E]]
+[[Category: Didierjean C]]
-[[Category: Girardet, J M]]
+[[Category: Favier F]]
-[[Category: Hecker, A]]
+[[Category: Gelhaye E]]
-[[Category: Morel-Rouhier, M]]
+[[Category: Girardet JM]]
-[[Category: Schwartz, M]]
+[[Category: Hecker A]]
-[[Category: Ecm4]]
+[[Category: Morel-Rouhier M]]
-[[Category: Glutathione]]
+[[Category: Schwartz M]]
-[[Category: Glutathione transferase]]
-[[Category: Glutathionyl-hydroquinone reductase]]
-[[Category: Quinone]]
-[[Category: Saccharomyces cerevisiae]]
-[[Category: Transferase]]
-[[Category: Ykr076w]]

5lkb

From Proteopedia

Current revision

Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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