1pn9

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(New page: 200px<br /><applet load="1pn9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn9, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:1pn9.jpg|left|200px]]<br /><applet load="1pn9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pn9, resolution 2.00&Aring;" />
 
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'''Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae'''<br />
 
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==Overview==
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==Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae==
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Glutathione S-transferases (GSTs) are a major family of detoxification, enzymes which possess a wide range of substrate specificities. Most, organisms possess many GSTs belonging to multiple classes. Interest in, GSTs in insects is focused on their role in insecticide resistance; many, resistant insects have elevated levels of GST activity. In the malaria, vector Anopheles gambiae, elevated GST levels are associated with, resistance to the organochlorine insecticide DDT, [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane]. This mosquito is the, source of an insect GST, agGSTd1-6, which metabolizes DDT and is inhibited, by a number of pyrethroid insecticides. The crystal structure of agGSTd1-6, in complex with its inhibitor S-hexyl glutathione has been determined and, refined at 2.0 A resolution. The structure adopts a classical GST fold and, is similar to those of other insect delta-class GSTs, implying a common, conjugation mechanism. A structure-based model for the binding of DDT to, agGSTd1-6 reveals two subpockets in the hydrophobic binding site (H-site), each accommodating one planar p-chlorophenyl ring.
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<StructureSection load='1pn9' size='340' side='right'caption='[[1pn9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pn9]] is a 2 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=1PN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PN9 FirstGlance]. <br>
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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&#8491;</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=GTX:S-HEXYLGLUTATHIONE'>GTX</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=1pn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn9 OCA], [https://pdbe.org/1pn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pn9 RCSB], [https://www.ebi.ac.uk/pdbsum/1pn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GST1D_ANOGA GST1D_ANOGA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.<ref>PMID:9038148</ref> <ref>PMID:9164846</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pn/1pn9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pn9 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1PN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae] with GTX as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PN9 OCA].
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae., Chen L, Hall PR, Zhou XE, Ranson H, Hemingway J, Meehan EJ, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2211-7. Epub 2003, Nov 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14646079 14646079]
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__TOC__
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</StructureSection>
[[Category: Anopheles gambiae]]
[[Category: Anopheles gambiae]]
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[[Category: Glutathione transferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chen L]]
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[[Category: Chen, L.]]
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[[Category: Hall PR]]
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[[Category: Hall, P.R.]]
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[[Category: Hemingway J]]
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[[Category: Hemingway, J.]]
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[[Category: Meehan EJ]]
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[[Category: Meehan, E.J.]]
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[[Category: Ranson H]]
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[[Category: Ranson, H.]]
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[[Category: Zhou XE]]
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[[Category: Zhou, X.E.]]
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[[Category: GTX]]
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[[Category: protein inhibitor complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:56:26 2007''
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Current revision

Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae

PDB ID 1pn9

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