1TW9

Glutathione Transferase-2, apo form, from the nematode Heligmosomoides polygyrus

Summary for 1TW9

• Entry DOI: 10.2210/pdb1tw9/pdb
• Descriptor: glutathione S-transferase 2 (2 entities in total)
• Functional Keywords: transferase
• Biological source: Heligmosomoides polygyrus
• Total number of polymer chains: 8
• Total formula weight: 187334.62

Authors

Schuller, D.J.,Liu, Q.,Kriksunov, I.A.,Campbell, A.M.,Barrett, J.,Brophy, P.M.,Hao, Q. (deposition date: 2004-06-30, release date: 2004-08-03, Last modification date: 2023-08-23)

Primary citation

Schuller, D.J.,Liu, Q.,Kriksunov, I.A.,Campbell, A.M.,Barrett, J.,Brophy, P.M.,Hao, Q.
Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.
Proteins, 61:1024-1031, 2005

PubMed Abstract: The crystal structure of GST Nu2-2 (HpolGSTN2-2) from the model hookworm nematode Heligmosomoides polygyrus has been solved by the molecular replacement method and refined to a resolution of 1.71 A, providing the first structural data from a class of nematode-specific GSTs. By structural alignment with two Sigma class GSTs, glutathione could be rationally docked into the G-site of the enzyme. By comparing with all mammalian GST classes, a novel, long, and deep cleft was identified at the H-site, providing a potential site for ligand binding. This new GST class may support the establishment of infection parasitic nematodes by passively neutralizing chemical toxins derived from host environment. The structure serves as a starting point for structure-based drug/inhibitor design that would aim to selectively disrupt nematode chemical defenses.

PubMed: 16189827
DOI: 10.1002/prot.20649

Experimental method

X-RAY DIFFRACTION (1.71 Å)