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PDBsum entry 1oe7

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1oe7
Jmol
Contents
Protein chains
204 a.a. *
Ligands
GSH ×2
Waters ×225
* Residue conservation analysis
PDB id:
1oe7
Name: Transferase
Title: 28kda glutathione s-transferase from schistosoma haematobium
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)
Resolution:
1.8Å     R-factor:   0.229     R-free:   0.289
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
Date:
19-Mar-03     Release date:   25-Jul-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P30114  (GST28_SCHHA) -  Glutathione S-transferase class-mu 28 kDa isozyme
Seq:
Struc:
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.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+
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!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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
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.