4yh2
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Glutathione Transferase E6 from Drosophila melanogaster== |
| + | <StructureSection load='4yh2' size='340' side='right' caption='[[4yh2]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4yh2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YH2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | ||
| + | <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> | ||
| + | <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=4yh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yh2 OCA], [http://pdbe.org/4yh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yh2 RCSB], [http://www.ebi.ac.uk/pdbsum/4yh2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Epsilon class glutathione transferases (GSTs) have been shown to contribute significantly to insecticide resistance. We report a new Epsilon class protein crystal structure from Drosophila melanogaster for the glutathione transferase DmGSTE6. The structure reveals a novel Epsilon clasp motif that is conserved across hundreds of millions of years of evolution of the insect Diptera order. This histidine-serine motif lies in the subunit interface and appears to contribute to quaternary stability as well as directly connecting the two glutathiones in the active sites of this dimeric enzyme. | ||
| - | + | Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site.,Wongsantichon J, Robinson RC, Ketterman AJ Biosci Rep. 2015 Oct 20;35(6). pii: e00272. doi: 10.1042/BSR20150183. PMID:26487708<ref>PMID:26487708</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4yh2" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glutathione transferase]] | ||
| + | [[Category: Ketterman, A J]] | ||
| + | [[Category: Robinson, R C]] | ||
[[Category: Wongsantichon, J]] | [[Category: Wongsantichon, J]] | ||
| - | [[Category: | + | [[Category: Drosophila]] |
| - | [[Category: | + | [[Category: Transferase]] |
Revision as of 17:12, 10 February 2016
Glutathione Transferase E6 from Drosophila melanogaster
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