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

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: 14646079
DOI: 10.1107/S0907444903018493

Experimental method

X-RAY DIFFRACTION (2 Å)