1jlw
From Proteopedia
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Anopheles dirus species B glutathione S-transferases 1-4
Overview
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, of the Anopheles GSTs to be enclosed. The glutathione-binding helix alpha2, and flanking residues are disordered in the AdGST1-4 (apo) structure, yet, ordered in the AdGST1-3 (GSH-bound) structure, suggesting that insect GSTs, operate with an induced fit mechanism similar to that found in the plant, phi- and human pi-class GSTs. Despite the high overall sequence, identities, the active site residues of AdGST1-4 and AdGST1-3 have, different conformations.
About this Structure
1JLW is a Single protein structure of sequence from Anopheles cracens. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B., Oakley AJ, Harnnoi T, Udomsinprasert R, Jirajaroenrat K, Ketterman AJ, Wilce MC, Protein Sci. 2001 Nov;10(11):2176-85. PMID:11604524
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