Research Article

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

  1. David J. Schuller1,2,†,
  2. Qun Liu1,2,†,
  3. Irina A. Kriksunov1,2,
  4. Alison M. Campbell3,
  5. John Barrett3,
  6. Peter M. Brophy3,
  7. Quan Hao1,2,*

Article first published online: 27 SEP 2005

DOI: 10.1002/prot.20649

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 61, Issue 4, pages 1024–1031, 1 December 2005

Additional Information

How to Cite

Schuller, D. J., Liu, Q., Kriksunov, I. A., Campbell, A. M., Barrett, J., Brophy, P. M. and Hao, Q. (2005), Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus. Proteins: Structure, Function, and Bioinformatics, 61: 1024–1031. doi: 10.1002/prot.20649

Author Information

  1. 1

    Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York

  2. 2

    MacCHESS, Cornell University, Ithaca, New York

  3. 3

    Institute of Biological Sciences, University of Wales, Aberystwyth, Ceredigion, Wales, United Kingdom

  1. †

    Both authors contributed equally to this work.

*MacCHESS, Cornell University, Ithaca, NY 14853-8001

Publication History

  1. Issue published online: 17 NOV 2005
  2. Article first published online: 27 SEP 2005
  3. Manuscript Accepted: 16 MAY 2005
  4. Manuscript Received: 1 FEB 2005

Funded by

  • BBSRC UK. Grant Number: S14953
  • National Institutes of Health (National Center for Research Resources). Grant Number: RR-01646
  • National Science Foundation. Grant Number: DMR 02-25180

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Keywords:

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

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. Proteins 2005. © 2005 Wiley-Liss, Inc.

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