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

Aaron J. Oakley, Thasaneeya Harnnoi, Rungrutai Udomsinprasert, Kanya Jirajaroenrat, Albert J. Ketterman, Matthew C.J. Wilce

研究成果: ジャーナルへの寄稿学術誌査読

73 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)2176-2185
ページ数10
ジャーナルProtein Science
10
11
DOI
出版ステータス出版済み - 11月 1 2001

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学

フィンガープリント

「The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル