Literature summary for 2.5.1.18 extracted from

Wang, Y.; Qiu, L.; Ranson, H.; Lumjuan, N.; Hemingway, J.; Setzer, W.N.; Meehan, E.J.; Chen, L.
Structure of an insect epsilon class glutathione S-transferase from the malaria vector Anopheles gambiae provides an explanation for the high DDT-detoxifying activity (2008), J. Struct. Biol., 164, 228-235.

Crystallization (Commentary)

Crystallization (Comment)	Organism
three agGSTe2 crystal structures including one apo form and two binary complex forms with the co-factor glutathione or the inhibitor S-hexylglutathione, sitting-drop vapor diffusion, 20°C, protein solution is mixed with an equal volume of a reservoir solution, containing 0.1 M Bis-Tris buffer, pH 6.5, and 25% w/v PEG 3350 for the apoenzyme crystallization, or for the enzyme-glutathione complex containing 0.2 M ammonium acetate, 0.1 M sodium acetate buffer, pH 4.6, and 30% w/v PEG 4000, or for the enzyme-inhibitor complex containing 0.2 M sodium iodide and 20% w/v PEG 3350, pH 6.9, 3 weeks, X-ray diffraction structure determination and analysis at 1.4-2.2 A resolution, molecular replacement method	Anopheles gambiae

Crystallization (Comment)

Organism

three agGSTe2 crystal structures including one apo form and two binary complex forms with the co-factor glutathione or the inhibitor S-hexylglutathione, sitting-drop vapor diffusion, 20°C, protein solution is mixed with an equal volume of a reservoir solution, containing 0.1 M Bis-Tris buffer, pH 6.5, and 25% w/v PEG 3350 for the apoenzyme crystallization, or for the enzyme-glutathione complex containing 0.2 M ammonium acetate, 0.1 M sodium acetate buffer, pH 4.6, and 30% w/v PEG 4000, or for the enzyme-inhibitor complex containing 0.2 M sodium iodide and 20% w/v PEG 3350, pH 6.9, 3 weeks, X-ray diffraction structure determination and analysis at 1.4-2.2 A resolution, molecular replacement method

Anopheles gambiae

Inhibitors

Inhibitors	Comment	Organism	Structure
S-hexylglutathione	inhibitor binding does not induce significant conformational changes in the protein	Anopheles gambiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione	Anopheles gambiae	detoxification of the insecticide DDT, especially by isozyme agGSTe2	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Anopheles gambiae	Q93113	epsilon class isozyme agGSTe2	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione	detoxification of the insecticide DDT, especially by isozyme agGSTe2	Anopheles gambiae	?	-	?
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione	i.e. DDT, modeling of DDT into the putative DDT-binding pocket, catalytic mechanism of isozyme agGSTe2 that shows high activity through the inclination of the upper part of H4 helix, H4'' helix, which brings residues Arg112, Glu116, and Phe120 closer to the GSH-binding site resulting in a more efficient GS- stabilizing hydrogen-bond-network and higher DDT-binding affinity, overview	Anopheles gambiae	1,1-dichloro-2,2-bis-(4-chlorophenyl)ethylene + ?	product formation through an elimination reaction triggered by the nucleophilic attack of the thiolate group of GS- on the beta-hydrogen of DDT	?
additional information	agGSTe2 has a long narrow cleft at the interface of the N- and C-domains, in which a GSH molecule tightly fits, binding of glutathione does not induce significant conformational changes in the isozyme agGSTe2 protein, structure, overview	Anopheles gambiae	?	-	?

Subunits

Subunits	Comment	Organism
More	agGSTe2 is a canonical GST fold with a highly conserved N-domain and a less conserved C-domain, isozyme agGSTe2 amino acid sequence and secondary structure comparisons, overview	Anopheles gambiae

Synonyms

Synonyms	Comment	Organism
agGSTe2	-	Anopheles gambiae
epsilon class GST	-	Anopheles gambiae
glutathione S-transferase	-	Anopheles gambiae
GST	-	Anopheles gambiae