3wyw
From Proteopedia
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| - | ''' | + | ==Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase== |
| + | <StructureSection load='3wyw' size='340' side='right' caption='[[3wyw]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </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> | ||
| + | <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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Nilaparvata lugens]] | ||
| + | [[Category: Higashiura, A]] | ||
| + | [[Category: Nakagawa, A]] | ||
[[Category: Yamamoto, K]] | [[Category: Yamamoto, K]] | ||
| - | [[Category: | + | [[Category: Glutathione]] |
| - | [[Category: | + | [[Category: Glutathione conjugation]] |
| + | [[Category: Transferase]] | ||
Revision as of 13:35, 14 January 2015
Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase
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