1pn9
From Proteopedia
(New page: 200px<br /><applet load="1pn9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn9, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1pn9.jpg|left|200px]]<br /><applet load="1pn9" size=" | + | [[Image:1pn9.jpg|left|200px]]<br /><applet load="1pn9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pn9, resolution 2.00Å" /> | caption="1pn9, resolution 2.00Å" /> | ||
'''Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae'''<br /> | '''Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glutathione S-transferases (GSTs) are a major family of detoxification | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=GTX:'>GTX</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Hall, P | + | [[Category: Hall, P R.]] |
[[Category: Hemingway, J.]] | [[Category: Hemingway, J.]] | ||
| - | [[Category: Meehan, E | + | [[Category: Meehan, E J.]] |
[[Category: Ranson, H.]] | [[Category: Ranson, H.]] | ||
| - | [[Category: Zhou, X | + | [[Category: Zhou, X E.]] |
[[Category: GTX]] | [[Category: GTX]] | ||
[[Category: protein inhibitor complex]] | [[Category: protein inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:36 2008'' |
Revision as of 12:30, 21 February 2008
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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
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 with as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 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
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