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4g19

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==Crystal structure of the glutathione transferase GTE1 from Phanerochaete chrysosporium in complex with glutathione==
==Crystal structure of the glutathione transferase GTE1 from Phanerochaete chrysosporium in complex with glutathione==
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<StructureSection load='4g19' size='340' side='right' caption='[[4g19]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4g19' size='340' side='right'caption='[[4g19]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g19]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysosporium_pruinosum_(gilman_&_abbott)_carmich. Chrysosporium pruinosum (gilman & abbott) carmich.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G19 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g19]] is a 4 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=4G19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G19 FirstGlance]. <br>
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</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=GOL:GLYCEROL'>GOL</scene>, <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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f03|4f03]]</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>
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<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=4g19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g19 OCA], [http://pdbe.org/4g19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g19 RCSB], [http://www.ebi.ac.uk/pdbsum/4g19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g19 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g19 OCA], [https://pdbe.org/4g19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g19 RCSB], [https://www.ebi.ac.uk/pdbsum/4g19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g19 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/I6ZUH3_PHACH I6ZUH3_PHACH]
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Glutathione S-transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. A new fungal specific class of GST has been highlighted by genomic approaches. The biochemical and structural characterization of one isoform of this class in Phanerochaete chrysosporium revealed original properties. The three-dimensional structure showed a new dimerization mode and specific features by comparison with the canonical GST structure. An additional beta-hairpin motif in the N-terminal domain prevents the formation of the regular GST dimer and acts as a lid, which closes upon glutathione binding. Moreover, this isoform is the first described GST that contains all secondary structural elements, including helix alpha4' in the C-terminal domain, of the presumed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2). A sulfate binding site has been identified close to the glutathione binding site and allows the binding of 8-anilino-1-naphtalene sulfonic acid. Competition experiments between 8-anilino-1-naphtalene sulfonic acid, which has fluorescent properties, and various molecules showed that this GST binds glutathionylated and sulfated compounds but also wood extractive molecules, such as vanillin, chloronitrobenzoic acid, hydroxyacetophenone, catechins, and aldehydes, in the glutathione pocket. This enzyme could thus function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it could also act as a ligandin of wood extractive compounds. These new structural and functional properties lead us to propose that this GST belongs to a new class that we name GSTFuA, for fungal specific GST class A.
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Characterization of a Phanerochaete chrysosporium Glutathione Transferase Reveals a Novel Structural and Functional Class with Ligandin Properties.,Mathieu Y, Prosper P, Buee M, Dumarcay S, Favier F, Gelhaye E, Gerardin P, Harvengt L, Jacquot JP, Lamant T, Meux E, Mathiot S, Didierjean C, Morel M J Biol Chem. 2012 Nov 9;287(46):39001-11. doi: 10.1074/jbc.M112.402776. Epub 2012, Sep 24. PMID:23007392<ref>PMID:23007392</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 4g19" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Glutathione S-transferase|Glutathione S-transferase]]
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Didierjean, C]]
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[[Category: Large Structures]]
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[[Category: Favier, F]]
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Prosper, P]]
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[[Category: Didierjean C]]
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[[Category: Glutathione]]
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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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Current revision

Crystal structure of the glutathione transferase GTE1 from Phanerochaete chrysosporium in complex with glutathione

PDB ID 4g19

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