Premium
Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus
Author(s) -
Schuller David J.,
Liu Qun,
Kriksunov Irina A.,
Campbell Alison M.,
Barrett John,
Brophy Peter M.,
Hao Quan
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20649
Subject(s) - nematode , heligmosomoides polygyrus , biology , glutathione , ligand (biochemistry) , biochemistry , enzyme , ecology , receptor
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 Å, 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. Proteins 2005. © 2005 Wiley‐Liss, Inc.