PDBsum entry 1tw9

Go to PDB code: 
protein Protein-protein interface(s) links
Transferase PDB id
Protein chains
(+ 1 more) 191 a.a. *
205 a.a. *
Waters ×1860
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Glutathione transferase-2, apo form, from the nematode helig polygyrus
Structure: Glutathione s-transferase 2. Chain: a, b, c, d, e, f, g, h. Engineered: yes
Source: Heligmosomoides polygyrus. Organism_taxid: 6339. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
1.71Å     R-factor:   0.181     R-free:   0.232
Authors: D.J.Schuller,Q.Liu,I.A.Kriksunov,A.M.Campbell,J.Barrett,P.M. Q.Hao
Key ref:
D.J.Schuller et al. (2005). Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus. Proteins, 61, 1024-1031. PubMed id: 16189827 DOI: 10.1002/prot.20649
30-Jun-04     Release date:   03-Aug-04    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9NJQ6  (Q9NJQ6_9BILA) -  Glutathione S-transferase 2 (Fragment)
204 a.a.
191 a.a.*
Protein chain
Pfam   ArchSchema ?
Q9NJQ6  (Q9NJQ6_9BILA) -  Glutathione S-transferase 2 (Fragment)
204 a.a.
205 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 11 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     1 term  


DOI no: 10.1002/prot.20649 Proteins 61:1024-1031 (2005)
PubMed id: 16189827  
Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.
D.J.Schuller, Q.Liu, I.A.Kriksunov, A.M.Campbell, J.Barrett, P.M.Brophy, Q.Hao.
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.
  Selected figure(s)  
Figure 1.
Figure 1. Structural alignment of eight rHpolGSTN2-2 molecules in the crystallographic asymmetric unit. Side-chains at three regions with large structural variations are shown besides the C trace. Color scheme: chain A, red; chain B, dark green; chain C, blue; chain D, yellow; chain E, cyan; chain F, magenta; chain G, orange; chain H, gray. All figures, if not otherwise specified, were prepared with Molscript[25] or Pymol ( and rendered by PovRay (
Figure 2.
Figure 2. Ribbon representation of rHpolGSTN2-2 homodimer.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 61, 1024-1031) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21428697 A.Oakley (2011).
Glutathione transferases: a structural perspective.
  Drug Metab Rev, 43, 138-151.  
20923271 A.R.Jariwala, L.M.Oliveira, D.J.Diemert, B.Keegan, J.L.Plieskatt, M.V.Periago, M.E.Bottazzi, P.J.Hotez, and J.M.Bethony (2010).
Potency testing for the experimental Na-GST-1 hookworm vaccine.
  Expert Rev Vaccines, 9, 1219-1230.  
20145100 B.Zhan, S.Perally, P.M.Brophy, J.Xue, G.Goud, S.Liu, V.Deumic, Oliveira, J.Bethony, M.E.Bottazzi, D.Jiang, P.Gillespie, S.H.Xiao, R.Gupta, A.Loukas, N.Ranjit, S.Lustigman, Y.Oksov, and P.Hotez (2010).
Molecular cloning, biochemical characterization, and partial protective immunity of the heme-binding glutathione S-transferases from the human hookworm Necator americanus.
  Infect Immun, 78, 1552-1563.  
20948553 P.J.Hotez, J.M.Bethony, D.J.Diemert, M.Pearson, and A.Loukas (2010).
Developing vaccines to combat hookworm infection and intestinal schistosomiasis.
  Nat Rev Microbiol, 8, 814-826.  
20686661 S.Severance, A.Rajagopal, A.U.Rao, G.C.Cerqueira, M.Mitreva, N.M.El-Sayed, M.Krause, and I.Hamza (2010).
Genome-wide analysis reveals novel genes essential for heme homeostasis in Caenorhabditis elegans.
  PLoS Genet, 6, e1001044.  
19265562 J.Barrett (2009).
Forty years of helminth biochemistry.
  Parasitology, 136, 1633-1642.  
17973970 D.M.Kristan (2007).
Chronic calorie restriction increases susceptibility of laboratory mice (Mus musculus) to a primary intestinal parasite infection.
  Aging Cell, 6, 817-825.  
17692078 G.Dubreuil, M.Magliano, E.Deleury, P.Abad, and M.N.Rosso (2007).
Transcriptome analysis of root-knot nematode functions induced in the early stages of parasitism.
  New Phytol, 176, 426-436.  
17594497 O.A.Asojo, K.Homma, M.Sedlacek, M.Ngamelue, G.N.Goud, B.Zhan, V.Deumic, O.Asojo, and P.J.Hotez (2007).
X-ray structures of Na-GST-1 and Na-GST-2 two glutathione S-transferase from the human hookworm Necator americanus.
  BMC Struct Biol, 7, 42.
PDB codes: 2on5 2on7
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.