9C0A

Sigma class glutathione transferase from Taenia solium 1.75 A

Summary for 9C0A

• Entry DOI: 10.2210/pdb9c0a/pdb
• Descriptor: Sigma-type glutathione S-transferase, DI(HYDROXYETHYL)ETHER, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: glutathione, glutathione transferase sigma class, taenia solium, detoxification system., immune system
• Biological source: Taenia solium (pork tapeworm)
• Total number of polymer chains: 1
• Total formula weight: 24953.11

Authors

Miranda-Blancas, R.,Cardona-Echavarria, M.C.,Garcia-Gutierrez, P.,Sanchez-Juarez, C.,Flores-Lopez, R.,Zubillaga, R.,Rodriguez-Lima, O.,Sanchez-Perez, L.C.,Landa, A.,Rudino-Pinera, E. (deposition date: 2024-05-24, release date: 2025-06-11)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)