9DDL

Glutathione transferase sigma class from Taenia solium 1.3

9DDL の概要

• エントリーDOI: 10.2210/pdb9ddl/pdb
• 関連するPDBエントリー: 9C0A
• 分子名称: Sigma-type glutathione S-transferase, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: glutathione transferase, prostaglandine d2 syntase, glutathione transferase sigma class, taenia solium, transferase
• 由来する生物種: Taenia solium (pork tapeworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24432.54

構造登録者

Miranda-Blancas, R.,Cardona-Echavarria, M.C.,Sanchez, C.,Sanchez-Perez, L.C.,Flores-Lopez, R.,Rodriguez-Lima, O.,Garcia-Gutierrez, P.,Zubillaga, R.,Landa, A.,Rudino-Pinera, E. (登録日: 2024-08-28, 公開日: 2025-06-11)

主引用文献

Miranda-Blancas, R.,Garcia-Gutierrez, P.,Sanchez-Juarez, C.,Cardona-Echavarria, M.C.,Flores-Lopez, R.,Zubillaga, R.A.,Rodriguez-Lima, O.,Sanchez-Perez, L.C.,Rudino-Pinera, E.,Landa, A.
Structural insights into sigma class glutathione transferase from Taenia solium: Analysis and functional implications.
Plos Negl Trop Dis, 19:e0013024-e0013024, 2025

PubMed Abstract: Neglected tropical diseases pose a significant threat to global health, especially in low- and middle-income countries where treatment options are inadequate and transmission risk factors persist. One example is neurocysticercosis caused by Taenia solium. Sigma class glutathione transferases (Sigma GSTs) are key regulators of Th1 inflammatory responses, making them promising targets for development of therapies and vaccines. This study presents the first report on the crystallographic structures of recombinant 24-kDa sigma class GST from T. solium (rTs24GST), which were determined at resolutions of 1.30 and 1.75 Å. The apo-form structures show the typical GST fold with distinct N- and C-terminal domains and highlight regions of notable flexibility near the G-site. Molecular dynamics simulations show that the presence of glutathione stabilizes the enzyme and reduces conformational fluctuations. Comparative analysis with other GSTs revealed conserved flexible regions that correlate with glutathione binding. These structural insights into rTs24GST can be associated with evolutionary adaptations for interacting with diverse substrates and could open new avenues for developing inhibitors and therapeutic strategies against neurocysticercosis.

PubMed: 40445974
DOI: 10.1371/journal.pntd.0013024

実験手法

X-RAY DIFFRACTION (1.3 Å)