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PDBsum entry 3fhs

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3fhs
Jmol
Contents
Protein chains
216 a.a. *
Ligands
GSH ×2
Waters ×100
* Residue conservation analysis
Superseded by: 4top
PDB id:
3fhs
Name: Transferase
Title: Glutathione transferase from glycine max at 2.7 resolution
Structure: 2,4-d inducible glutathione s-transferase. Chain: a, b. Engineered: yes
Source: Glycine max. Soybean. Organism_taxid: 3847. Gene: gst 4(gmgst4-4), gsta. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.71Å     R-factor:   0.192     R-free:   0.241
Authors: I.Axarli,D.Prathusha,A.C.Papageorgiou,N.E.Labrou
Key ref: I.Axarli et al. (2009). Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases. Biochem J, 422, 247-256. PubMed id: 19538182
Date:
10-Dec-08     Release date:   07-Jul-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O49235  (O49235_SOYBN) -  2,4-D inducible glutathione S-transferase
Seq:
Struc:
219 a.a.
216 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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

 

 
    reference    
 
 
Biochem J 422:247-256 (2009)
PubMed id: 19538182  
 
 
Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases.
I.Axarli, P.Dhavala, A.C.Papageorgiou, N.E.Labrou.
 
  ABSTRACT  
 
Cytosolic GSTs (glutathione transferases) are a multifunctional group of enzymes widely distributed in Nature and involved in cellular detoxification processes. The three-dimensional structure of GmGSTU4-4 (Glycine max GST Tau 4-4) complexed with GSH was determined by the molecular replacement method at 2.7 A (1 A=0.1 nm) resolution. The bound GSH is located in a region formed by the beginning of alpha-helices H1, H2 and H3 in the N-terminal domain of the enzyme. Significant differences in the G-site (GSH-binding site) as compared with the structure determined in complex with Nb-GSH [S-(p-nitrobenzyl)-glutathione] were found. These differences were identified in the hydrogen-bonding and electrostatic interaction pattern and, consequently, GSH was found bound in two different conformations. In one subunit, the enzyme forms a complex with the ionized form of GSH, whereas in the other subunit it can form a complex with the non-ionized form. However, only the ionized form of GSH may form a productive and catalytically competent complex. Furthermore, a comparison of the GSH-bound structure with the Nb-GSH-bound structure shows a significant movement of the upper part of alpha-helix H4 and the C-terminal. This indicates an intrasubunit modulation between the G-site and the H-site (electrophile-binding site), suggesting that the enzyme recognizes the xenobiotic substrates by an induced-fit mechanism. The reorganization of Arg111 and Tyr107 upon xenobiotic substrate binding appears to govern the intrasubunit structural communication between the G- and H-site and the binding of GSH. The structural observations were further verified by steady-state kinetic analysis and site-directed mutagenesis studies.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21425939 I.Cummins, D.P.Dixon, S.Freitag-Pohl, M.Skipsey, and R.Edwards (2011).
Multiple roles for plant glutathione transferases in xenobiotic detoxification.
  Drug Metab Rev, 43, 266-280.  
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