1v2a
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Glutathione S-transferase 1-6 from Anopheles dirus species B
OverviewOverview
The insect GST (glutathione transferase) supergene family encodes a varied, group of proteins belonging to at least six individual classes. Interest, in insect GSTs has focused on their role in conferring insecticide, resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for, structural as well as enzyme activities. We have obtained a new Delta, class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The, adGSTD5-5 isoenzyme was identified and was only detectably expressed in A., dirus adult females. A putative promoter analysis suggests that this GST, has an involvement in oogenesis. The enzyme displayed little activity for, classical GST substrates, although it possessed the greatest activity for, DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta, GSTs. However, GST activity was inhibited or enhanced in the presence of, various fatty acids, suggesting that the enzyme may be modulated by fatty, acids. We obtained a crystal structure for adGSTD5-5 and compared it with, other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and, more polar active-site topology.
About this StructureAbout this Structure
1V2A is a Single protein structure of sequence from Anopheles dirus with GTS as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
ReferenceReference
Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme., Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ, Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:15717864
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