Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus

David J. Schuller, Qun Liu, Irina A. Kriksunov, Alison Mary Campbell, John Barrett, Peter M. Brophy, Quan Hao

Research output: Contribution to journalArticlepeer-review

30 Citations (SciVal)

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 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.
Original languageEnglish
Pages (from-to)1024-1031
Number of pages8
JournalProteins: Structure, Function and Genetics
Volume61
Issue number4
Early online date27 Sept 2005
DOIs
Publication statusPublished - 01 Dec 2005

Keywords

  • Keywords: glutathione transferase Nu2-2
  • molecular replacement method
  • ligand binding
  • crystal structure

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