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1pn9

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Revision as of 16:07, 11 September 2015

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

Structural highlights

1pn9 is a 2 chain structure with sequence from Anoga. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	GST1-6 (ANOGA)
Activity:	Glutathione transferase, with EC number 2.5.1.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GST1D_ANOGA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:14646079^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ranson H, Cornel AJ, Fournier D, Vaughan A, Collins FH, Hemingway J. Cloning and localization of a glutathione S-transferase class I gene from Anopheles gambiae. J Biol Chem. 1997 Feb 28;272(9):5464-8. PMID:9038148
↑ Ranson H, Prapanthadara La, Hemingway J. Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae. Biochem J. 1997 May 15;324 ( Pt 1):97-102. PMID:9164846
↑ Chen L, Hall PR, Zhou XE, Ranson H, Hemingway J, Meehan EJ. Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2211-7. Epub 2003, Nov 27. PMID:14646079

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pn9"

@@ Line 2: / Line 2: @@
 <StructureSection load='1pn9' size='340' side='right' caption='[[1pn9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pn9]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PN9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pn9]] is a 2 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=1PN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PN9 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 Anopheles gambiae])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 ANOGA])</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=1pn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pn9 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn9 PDBsum]</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=1pn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn9 OCA], [http://pdbe.org/1pn9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pn9 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn9 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GSTT6_ANOGA GSTT6_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>
+[[http://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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1pn9" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Anopheles gambiae]]
+[[Category: Anoga]]
 [[Category: Glutathione transferase]]
 [[Category: Chen, L]]

1pn9

From Proteopedia

Revision as of 16:07, 11 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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