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1pn9

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[[Image:1pn9.jpg|left|200px]]
[[Image:1pn9.jpg|left|200px]]
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{{Structure
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|PDB= 1pn9 |SIZE=350|CAPTION= <scene name='initialview01'>1pn9</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1pn9", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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|GENE= GST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 Anopheles gambiae])
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{{STRUCTURE_1pn9| PDB=1pn9 | SCENE= }}
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1pn9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pn9 RCSB]</span>
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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'''
'''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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[[Category: Ranson, H.]]
[[Category: Ranson, H.]]
[[Category: Zhou, X E.]]
[[Category: Zhou, X E.]]
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[[Category: protein inhibitor complex]]
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[[Category: Protein inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:16:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:58 2008''
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Revision as of 02:16, 3 May 2008

Template:STRUCTURE 1pn9

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


Overview

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.

About this Structure

1PN9 is a Single protein structure of sequence from Anopheles gambiae. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 05:16:29 2008

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