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3wyw

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==Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase==
==Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase==
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<StructureSection load='3wyw' size='340' side='right' caption='[[3wyw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='3wyw' size='340' side='right'caption='[[3wyw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wyw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nilaparvata_lugens Nilaparvata lugens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WYW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3wyw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nilaparvata_lugens Nilaparvata lugens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYW 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=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.7&#8491;</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=3wyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wyw RCSB], [http://www.ebi.ac.uk/pdbsum/3wyw PDBsum]</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=EDO:1,2-ETHANEDIOL'>EDO</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'>[https://proteopedia.org/fgij/fg.htm?mol=3wyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyw OCA], [https://pdbe.org/3wyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wyw RCSB], [https://www.ebi.ac.uk/pdbsum/3wyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wyw 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/Q8N0B3_NILLU Q8N0B3_NILLU]
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Glutathione transferases (GSTs) are a major class of detoxification enzymes that play a central role in the defense against environmental toxicants and oxidative stress. Here, we studied the crystal structure of a delta-class glutathione transferase from Nilaparvata lugens, nlGSTD, to gain insights into its catalytic mechanism. The structure of nlGSTD in complex with glutathione, determined at a resolution of 1.7A, revealed that it exists as a dimer and its secondary and tertiary structures are similar to those of other delta-class GSTs. Analysis of a complex between nlGSTD and glutathione showed that the bound glutathione was localized to the glutathione-binding site. Site-directed mutagenesis of nlGSTD mutants indicated that amino acid residues Ser11, His52, Glu66, and Phe119 contribute to catalytic activity.
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Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase.,Yamamoto K, Higashiura A, Hossain MT, Yamada N, Shiotsuki T, Nakagawa A Arch Biochem Biophys. 2014 Dec 9;566C:36-42. doi: 10.1016/j.abb.2014.12.001. PMID:25497345<ref>PMID:25497345</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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==See Also==
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</div>
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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: Large Structures]]
[[Category: Nilaparvata lugens]]
[[Category: Nilaparvata lugens]]
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[[Category: Higashiura, A]]
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[[Category: Higashiura A]]
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[[Category: Nakagawa, A]]
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[[Category: Nakagawa A]]
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[[Category: Yamamoto, K]]
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[[Category: Yamamoto K]]
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[[Category: Glutathione]]
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[[Category: Glutathione conjugation]]
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[[Category: Transferase]]
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Current revision

Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase

PDB ID 3wyw

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