3ppu

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<StructureSection load='3ppu' size='340' side='right'caption='[[3ppu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3ppu' size='340' side='right'caption='[[3ppu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ppu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ppu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPU FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3ppu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppu OCA], [https://pdbe.org/3ppu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppu RCSB], [https://www.ebi.ac.uk/pdbsum/3ppu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppu 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=3ppu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppu OCA], [https://pdbe.org/3ppu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppu RCSB], [https://www.ebi.ac.uk/pdbsum/3ppu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppu ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B3VQJ7_PHACH B3VQJ7_PHACH]
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The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.
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Glutathione transferases of Phanerochaete chrysosporium: S-glutathionyl-p-hydroquinone reductase belongs to a new structural class.,Meux E, Prosper P, Ngadin A, Didierjean C, Morel M, Dumarcay S, Lamant T, Jacquot JP, Favier F, Gelhaye E J Biol Chem. 2011 Mar 18;286(11):9162-73. Epub 2010 Dec 22. PMID:21177852<ref>PMID:21177852</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ppu" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Didierjean, C]]
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Favier, F]]
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[[Category: Didierjean C]]
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[[Category: Prosper, P]]
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[[Category: Favier F]]
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[[Category: Gst fold]]
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[[Category: Prosper P]]
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[[Category: Transferase]]
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Revision as of 13:33, 1 March 2024

Crystal structure of the glutathione-S-transferase Xi from Phanerochaete chrysosporium

PDB ID 3ppu

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