1PN9
Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae
Summary for 1PN9
Entry DOI | 10.2210/pdb1pn9/pdb |
Descriptor | Glutathione S-transferase 1-6, S-HEXYLGLUTATHIONE (3 entities in total) |
Functional Keywords | protein inhibitor complex, transferase |
Biological source | Anopheles gambiae (African malaria mosquito) |
Total number of polymer chains | 2 |
Total formula weight | 47724.47 |
Authors | Chen, L.,Hall, P.R.,Zhou, X.E.,Ranson, H.,Hemingway, J.,Meehan, E.J. (deposition date: 2003-06-12, release date: 2003-12-09, Last modification date: 2024-04-03) |
Primary citation | Chen, L.,Hall, P.R.,Zhou, X.E.,Ranson, H.,Hemingway, J.,Meehan, E.J. Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae. Acta Crystallogr.,Sect.D, 59:2211-2217, 2003 Cited by PubMed Abstract: 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. PubMed: 14646079DOI: 10.1107/S0907444903018493 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
