1JLV

Anopheles dirus species B glutathione S-transferases 1-3

1JLV の概要

• エントリーDOI: 10.2210/pdb1jlv/pdb
• 関連するPDBエントリー: 1JLV
• 分子名称: glutathione transferase GST1-3, GLUTATHIONE (3 entities in total)
• 機能のキーワード: glutathione s-transferase, gst, adgst1-3, transferase
• 由来する生物種: Anopheles cracens
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 144704.91

構造登録者

Oakley, A.J.,Harnnoi, T.,Udomsinprasert, R.,Jirajaroenrat, K.,Ketterman, A.J.,Wilce, M.C. (登録日: 2001-07-16, 公開日: 2002-07-16, 最終更新日: 2024-04-03)

主引用文献

Oakley, A.J.,Harnnoi, T.,Udomsinprasert, R.,Jirajaroenrat, K.,Ketterman, A.J.,Wilce, M.C.
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.
Protein Sci., 10:2176-2185, 2001

PubMed 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 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.

PubMed: 11604524
DOI: 10.1110/ps.21201

実験手法

X-RAY DIFFRACTION (1.75 Å)