PDBsum entry 1oe8

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protein ligands Protein-protein interface(s) links
Transferase PDB id
Jmol PyMol
Protein chains
204 a.a. *
GSH ×2
Waters ×316
* Residue conservation analysis
PDB id:
Name: Transferase
Title: 28kda glutathione s-transferase from schistosoma haematobium (glutathione saturated)
Structure: Glutathione s-transferase. Chain: a, b. Engineered: yes
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
1.65Å     R-factor:   0.229     R-free:   0.280
Authors: K.A.Johnson,F.Angelucci,D.Tsernoglou
Key ref:
K.A.Johnson et al. (2003). Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium. Biochemistry, 42, 10084-10094. PubMed id: 12939136 DOI: 10.1021/bi034449r
19-Mar-03     Release date:   25-Jul-03    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P30114  (GST28_SCHHA) -  Glutathione S-transferase class-mu 28 kDa isozyme
211 a.a.
204 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
Bound ligand (Het Group name = GSH)
corresponds exactly
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     transferase activity     2 terms  


DOI no: 10.1021/bi034449r Biochemistry 42:10084-10094 (2003)
PubMed id: 12939136  
Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium.
K.A.Johnson, F.Angelucci, A.Bellelli, M.Hervé, J.Fontaine, D.Tsernoglou, A.Capron, F.Trottein, M.Brunori.
Schistomiasis is a debilitating parasitic disease which affects 200 million people, causing life-threatening complications in 10% of the patients. This paper reports the crystal structure of the Schistosoma haematobium 28 kDa glutathione S-transferase, a multifunctional enzyme involved in host-parasite interactions and presently considered as a promising vaccine candidate against schistosomiasis. The structures of the GSH-free enzyme, as well as the partially (approximately 40%) and almost fully (approximately 80%) GSH-saturated enzyme, exhibit a unique feature, absent in previous GST structures, concerning the crucial and invariant Tyr10 side chain which occupies two alternative positions. The canonical conformer, which allows an H-bond to be formed between the side chain hydroxyl group and the activated thiolate of GSH, is somewhat less than 50% occupied. The new conformer, with the phenoxyl ring on the opposite side of the mobile loop connecting strand 1 and helix 1, is stabilized by a polar interaction with the guanidinium group of the conserved Arg21 side chain. The presence of two conformers of Tyr10 may provide a clue about clarifying the multiple catalytic functions of Sh28GST and might prove to be relevant for the design of specific antischistosomal drugs. The K(d) for GSH binding was determined by equilibrium fluorescence titrations to be approximately 3 microM and by stopped-flow rapid mixing experiments to be approximately 9 microM. The relatively tight binding of GSH by Sh28GST explains the residually bound GSH in the crystal and supports a possible role of GSH as a tightly bound cofactor involved in the catalytic mechanism for prostaglandin D(2) synthase activity.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21425928 J.U.Flanagan, and M.L.Smythe (2011).
Sigma-class glutathione transferases.
  Drug Metab Rev, 43, 194-214.  
18214950 J.Deville, J.Rey, and M.Chabbert (2008).
Comprehensive analysis of the helix-X-helix motif in soluble proteins.
  Proteins, 72, 115-135.  
17657508 T.Sakamoto, and T.Oikawa (2007).
Cubic crystal protein inclusions in the neodermis of the pancreatic fluke, Eurytrema pancreaticum, and Eurytrema coelomaticum.
  Parasitol Res, 101, 1393-1399.  
16154081 F.Angelucci, P.Baiocco, M.Brunori, L.Gourlay, V.Morea, and A.Bellelli (2005).
Insights into the catalytic mechanism of glutathione S-transferase: the lesson from Schistosoma haematobium.
  Structure, 13, 1241-1246.  
15640152 M.Perbandt, J.Höppner, C.Betzel, R.D.Walter, and E.Liebau (2005).
Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.
  J Biol Chem, 280, 12630-12636.
PDB codes: 1tu7 1tu8
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