PDBsum entry 1tu8

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Transferase PDB id
Protein chains
208 a.a. *
GTX ×4
Waters ×754
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Structure of onchoverca volvulus pi-class glutathione s- transferase with its kompetitive inhibitor s-hexyl-gsh
Structure: Glutathione s-transferase 2. Chain: a, b, c, d. Synonym: glutathione s-transferase, gst class-pi. Engineered: yes
Source: Onchocerca volvulus. Organism_taxid: 6282. Gene: gst2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
1.80Å     R-factor:   0.182     R-free:   0.217
Authors: M.Perbandt
Key ref:
M.Perbandt et al. (2005). Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus. J Biol Chem, 280, 12630-12636. PubMed id: 15640152 DOI: 10.1074/jbc.M413551200
24-Jun-04     Release date:   11-Jan-05    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P46427  (GSTP_ONCVO) -  Glutathione S-transferase 2
208 a.a.
208 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
Bound ligand (Het Group name = GTX)
matches with 76.00% similarity
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  


DOI no: 10.1074/jbc.M413551200 J Biol Chem 280:12630-12636 (2005)
PubMed id: 15640152  
Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.
M.Perbandt, J.Höppner, C.Betzel, R.D.Walter, E.Liebau.
Onchocerciasis is a debilitating parasitic disease caused by the filarial worm Onchocerca volvulus. Similar to other helminth parasites, O. volvulus is capable of evading the host's immune responses by a variety of defense mechanisms, including the detoxification activities of the glutathione S-transferases (GSTs). Additionally, in response to drug treatment, helminth GSTs are highly up-regulated, making them tempting targets both for chemotherapy and for vaccine development. We analyzed the three-dimensional x-ray structure of the major cytosolic GST from O. volvulus (Ov-GST2) in complex with its natural substrate glutathione and its competitive inhibitor S-hexylglutathione at 1.5 and 1.8 angstrom resolution, respectively. From the perspective of the biochemical classification, the Ov-GST2 seems to be related to pi-class GSTs. However, in comparison to other pi-class GSTs, in particular to the host's counterpart, the Ov-GST2 reveals significant and unusual differences in the sequence and overall structure. Major differences can be found in helix alpha-2, an important region for substrate recognition. Moreover, the binding site for the electrophilic co-substrate is spatially increased and more solvent-accessible. These structural alterations are responsible for different substrate specificities and will form the basis of parasite-specific structure-based drug design investigations.
  Selected figure(s)  
Figure 2.
FIG. 2. Ribbon diagram of Ov-GST2. The Ov-GST2 monomer emphasizing the secondary structural elements. Helices are colored light blue, -strands are green, and the 3[10] helices are dark blue. The S-hexylglutathione molecule bound to the active site is shown in ball-and-stick representation. The program RIBBONS (67) was used to produce the figure. N, N terminus.
Figure 5.
FIG. 5. Surface presentation of the active site from the human placenta -class GST with bound S-hexylglutathione shown as sticks (a) and the corresponding region of the O. volvulus GST2 (b). Here most of the H-site residues are exchanged, leading to a more solvent-accessible H-site. The program GRASP (61) was used to prepare the figure.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 12630-12636) copyright 2005.  
  Figures were selected by an automated process.