4gsn

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<StructureSection load='4gsn' size='340' side='right'caption='[[4gsn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='4gsn' size='340' side='right'caption='[[4gsn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gsn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Anoga Anoga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GSN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GSN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gsn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSN 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=1PE:PENTAETHYLENE+GLYCOL'>1PE</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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2il3|2il3]], [[2imi|2imi]]</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=1PE:PENTAETHYLENE+GLYCOL'>1PE</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=4gsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsn OCA], [http://pdbe.org/4gsn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gsn RCSB], [http://www.ebi.ac.uk/pdbsum/4gsn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsn 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=4gsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsn OCA], [https://pdbe.org/4gsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gsn RCSB], [https://www.ebi.ac.uk/pdbsum/4gsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsn 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/Q9GPL8_ANOGA Q9GPL8_ANOGA]
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The development of resistance to insecticides has become a classic exemplar of evolution occurring within human time scales. In this study we demonstrate how resistance to DDT in the major African malaria vector Anopheles gambiae is a result of both target-site resistance mechanisms that have introgressed between incipient species (the M- and S-molecular forms) and allelic variants in a DDT-detoxifying enzyme. Sequencing of the detoxification enzyme, Gste2, from DDT resistant and susceptible strains of An. gambiae, revealed a non-synonymous polymorphism (I114T), proximal to the DDT binding domain, which segregated with strain phenotype. Recombinant protein expression and DDT metabolism analysis revealed that the proteins from the susceptible strain lost activity at higher DDT concentrations, characteristic of substrate inhibition. The effect of I114T on GSTE2 protein structure was explored through X-ray crystallography. The amino acid exchange in the DDT-resistant strain introduced a hydroxyl group nearby the hydrophobic DDT-binding region. The exchange does not result in structural alterations but is predicted to facilitate local dynamics and enzyme activity. Expression of both wild-type and 114T alleles the allele in Drosophila conferred an increase in DDT tolerance. The 114T mutation was significantly associated with DDT resistance in wild caught M-form populations and acts in concert with target-site mutations in the voltage gated sodium channel (Vgsc-1575Y and Vgsc-1014F) to confer extreme levels of DDT resistance in wild caught An. gambiae.
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Metabolic and Target-Site Mechanisms Combine to Confer Strong DDT Resistance in Anopheles gambiae.,Mitchell SN, Rigden DJ, Dowd AJ, Lu F, Wilding CS, Weetman D, Dadzie S, Jenkins AM, Regna K, Boko P, Djogbenou L, Muskavitch MA, Ranson H, Paine MJ, Mayans O, Donnelly MJ PLoS One. 2014 Mar 27;9(3):e92662. doi: 10.1371/journal.pone.0092662. eCollection, 2014. PMID:24675797<ref>PMID:24675797</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 4gsn" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anoga]]
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[[Category: Anopheles gambiae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lu, F]]
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[[Category: Lu F]]
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[[Category: Mayans, O]]
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[[Category: Mayans O]]
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[[Category: Gst]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of GSTe2 ZAN/U variant from Anopheles gambiae

PDB ID 4gsn

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