1jlv
From Proteopedia
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Anopheles dirus species B glutathione S-transferases 1-3
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
1JLV is a Single protein structure of sequence from Anopheles cracens with GSH as ligand. 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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