4uss

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==Populus trichocarpa glutathione transferase X1-1 (GHR1), complexed with glutathione==
==Populus trichocarpa glutathione transferase X1-1 (GHR1), complexed with glutathione==
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<StructureSection load='4uss' size='340' side='right' caption='[[4uss]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4uss' size='340' side='right'caption='[[4uss]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4uss]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4USS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4USS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4uss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_trichocarpa Populus trichocarpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4USS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4USS 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=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.5&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></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=PO4:PHOSPHATE+ION'>PO4</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=4uss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uss OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uss RCSB], [http://www.ebi.ac.uk/pdbsum/4uss PDBsum]</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=4uss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uss OCA], [https://pdbe.org/4uss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uss RCSB], [https://www.ebi.ac.uk/pdbsum/4uss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uss ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glutathionyl-hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt-GHR1 and Pt-GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt-GHR2 localizes in nucleoids. At the structural level, Pt-GHR1 adopts a typical GHR fold, with a dimerization interface comparable to that of the bacterial and fungal GHR counterparts. Pt-GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms.
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Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.,Lallement PA, Meux E, Gualberto JM, Dumarcay S, Favier F, Didierjean C, Saul F, Haouz A, Morel-Rouhier M, Gelhaye E, Rouhier N, Hecker A FEBS Lett. 2014 Nov 29. pii: S0014-5793(14)00826-6. doi:, 10.1016/j.febslet.2014.11.021. PMID:25455804<ref>PMID:25455804</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 4uss" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutathione transferase]]
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[[Category: Large Structures]]
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[[Category: Didierjean, C]]
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[[Category: Populus trichocarpa]]
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[[Category: Dumaracay, S]]
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[[Category: Didierjean C]]
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[[Category: Favier, F]]
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[[Category: Dumaracay S]]
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[[Category: Gelhaye, E]]
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[[Category: Favier F]]
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[[Category: Gualberto, J M]]
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[[Category: Gelhaye E]]
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[[Category: Haouz, A]]
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[[Category: Gualberto JM]]
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[[Category: Hecker, A]]
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[[Category: Haouz A]]
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[[Category: Lallement, P A]]
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[[Category: Hecker A]]
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[[Category: Meux, E]]
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[[Category: Lallement PA]]
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[[Category: Morel-Rouhier, M]]
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[[Category: Meux E]]
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[[Category: Rouhier, N]]
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[[Category: Morel-Rouhier M]]
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[[Category: Saul, F]]
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[[Category: Rouhier N]]
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[[Category: Class xi]]
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[[Category: Saul F]]
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[[Category: Plastid]]
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[[Category: Poplar]]
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[[Category: Transferase]]
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Current revision

Populus trichocarpa glutathione transferase X1-1 (GHR1), complexed with glutathione

PDB ID 4uss

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