The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.

ABSTRACT: Glutathione S-transferases (GSTs) are dimeric proteins that play an important role in cellular detoxification. Four GSTs from the mosquito Anopheles dirus species B (Ad), an important malaria vector in South East Asia, are produced by alternate splicing of a single transcription product and were previously shown to have detoxifying activity towards pesticides such as DDT. We have determined the crystal structures for two of these alternatively spliced proteins, AdGST1-3 (complexed with glutathione) and AdGST1-4 (apo form), at 1.75 and 2.45 A resolution, respectively. These GST isozymes show differences from the related GST from the Australian sheep blowfly Lucilia cuprina; in particular, the presence of a C-terminal helix forming part of the active site. This helix causes the active site o

SUBMITTER: Oakley AJ 

PROVIDER: S-EPMC2374065 | biostudies-literature | 2001 Nov

REPOSITORIES: biostudies-literature