Publication: The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B
1
Issued Date
2001-11-01
Resource Type
ISSN
09618368
DOI
Other identifier(s)
2-s2.0-0034778978
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Protein Science. Vol.10, No.11 (2001), 2176-2185
Suggested Citation
Aaron J. Oakley, Thasaneeya Harnnoi, Rungrutai Udomsinprasert, Kanya Jirajaroenrat, Albert J. Ketterman, Matthew C.J. Wilce The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Protein Science. Vol.10, No.11 (2001), 2176-2185. doi:10.1110/ps.21201 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/26441
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B
Other Contributor(s)
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 Å 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 α2 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.