Crystallization and preliminary crystallographic analysis of a new class of glutathione transferase from nematodes.
Mouse and Heligmosomoides polygyrus constitute a readily manipulated small-animal laboratory model for investigating host-nematode interactions. Two major forms of glutathione transferase (GST) are expressed in H. polygyrus adult worms following primary infection. One of these forms belongs to a new class of GST which has only been found in the nematode phylum and therefore presents a possible target for nematode control. In this study, crystals were obtained of a recombinant representative of this new GST class from H. polygyrus. These crystals belong to the triclinic space group P1, with unit-cell parameters a = 72.7, b = 74.0, c = 88.6 A, alpha = 79.1, beta = 80.1, gamma = 81.5 degrees, and are likely to contain four homodimers in the asymmetric unit. X-ray diffraction data were collected to 1.8 A resolution on station A1 at the Cornell High-Energy Synchrotron Source (CHESS).
Kriksunov
I A
IA
MacCHESS at Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853-8001, USA.
Schuller
D J
DJ
Campbell
A M
AM
Barrett
J
J
Brophy
P M
PM
Hao
Q
Q
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D005982:Glutathione Transferase / Q000737:chemistry*; D015801:Helminth Proteins / Q000737:chemistry*; D009348:Nematoda / Q000201:enzymology*; D009351:Nematospiroides dubius / Q000201:enzymology; D011994:Recombinant Proteins
D015801:Helminth Proteins; D011994:Recombinant Proteins; D005982:Glutathione Transferase