PDBsum entry 2wgr

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protein ligands links
Oxidoreductase PDB id
Protein chain
163 a.a. *
Waters ×140
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Combining crystallography and molecular dynamics: the case of schistosoma mansoni phospholipid glutathione peroxidase
Structure: Glutathione peroxidase. Chain: a. Synonym: phospholipid-hydroperoxide glutathione peroxidase, gpx. Engineered: yes. Mutation: yes
Source: Schistosoma mansoni. Organism_taxid: 6183. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.70Å     R-factor:   0.183     R-free:   0.211
Authors: D.Dimastrogiovanni,M.Anselmi,A.E.Miele,G.Boumis,F.Angelucci, A.Di Nola,M.Brunori,A.Bellelli
Key ref: D.Dimastrogiovanni et al. (2010). Combining crystallography and molecular dynamics: the case of Schistosoma mansoni phospholipid glutathione peroxidase. Proteins, 78, 259-270. PubMed id: 19714775
24-Apr-09     Release date:   08-Sep-09    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q00277  (GPX1_SCHMA) -  Glutathione peroxidase
169 a.a.
163 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 peroxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
2 × glutathione
+ H(2)O(2)
= glutathione disulfide
+ 2 × H(2)O
      Cofactor: Se(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     oxidoreductase activity     3 terms  


Proteins 78:259-270 (2010)
PubMed id: 19714775  
Combining crystallography and molecular dynamics: the case of Schistosoma mansoni phospholipid glutathione peroxidase.
D.Dimastrogiovanni, M.Anselmi, A.E.Miele, G.Boumis, L.Petersson, F.Angelucci, A.D.Nola, M.Brunori, A.Bellelli.
Oxidative stress is a widespread challenge for living organisms, and especially so for parasitic ones, given the fact that their hosts can produce reactive oxygen species (ROS) as a mechanism of defense. Thus, long lived parasites, such as the flatworm Schistosomes, have evolved refined enzymatic systems capable of detoxifying ROS. Among these, glutathione peroxidases (Gpx) are a family of sulfur or selenium-dependent isozymes sharing the ability to reduce peroxides using the reducing equivalents provided by glutathione or possibly small proteins such as thioredoxin. As for other frontline antioxidant enzymatic systems, Gpxs are localized in the tegument of the Schistosomes, the outermost defense layer. In this article, we present the first crystal structure at 1.0 and 1.7 A resolution of two recombinant SmGpxs, carrying the active site mutations Sec43Cys and Sec43Ser, respectively. The structures confirm that this enzyme belongs to the monomeric class 4 (phospholipid hydroperoxide) Gpx. In the case of the Sec to Cys mutant, the catalytic Cys residue is oxidized to sulfonic acid. By combining static crystallography with molecular dynamics simulations, we obtained insight into the substrate binding sites and the conformational changes relevant to catalysis, proposing a role for the unusual reactivity of the catalytic residue.