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PDBsum entry 3ibh

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protein ligands links
Transferase PDB id
3ibh
Jmol
Contents
Protein chain
208 a.a. *
Ligands
GSH
Waters ×116
* Residue conservation analysis
PDB id:
3ibh
Name: Transferase
Title: Crystal structure of saccharomyces cerevisiae gtt2 in comple glutathione
Structure: Saccharomyces cerevisiae gtt2. Chain: a. Synonym: gst-ii. Engineered: yes
Source: Saccharomyces cerevisiae. Organism_taxid: 4932. Strain: s288c. Gene: gtt2, l0560, yll060c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.210     R-free:   0.247
Authors: X.X.Ma,Y.L.Jiang,Y.X.He,R.Bao,Y.X.Chen,C.Z.Zhou
Key ref: X.X.Ma et al. (2009). Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family. EMBO Rep, 10, 1320-1326. PubMed id: 19851333
Date:
15-Jul-09     Release date:   13-Oct-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q12390  (GST2_YEAST) -  Glutathione S-transferase 2
Seq:
Struc:
233 a.a.
208 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
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     glutathione metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
EMBO Rep 10:1320-1326 (2009)
PubMed id: 19851333  
 
 
Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.
X.X.Ma, Y.L.Jiang, Y.X.He, R.Bao, Y.Chen, C.Z.Zhou.
 
  ABSTRACT  
 
Glutathione-S-transferases (GSTs) are ubiquitous detoxification enzymes that catalyse the conjugation of electrophilic substrates to glutathione. Here, we present the crystal structures of Gtt2, a GST of Saccharomyces cerevisiae, in apo and two ligand-bound forms, at 2.23 A, 2.20 A and 2.10 A, respectively. Although Gtt2 has the overall structure of a GST, the absence of the classic catalytic essential residues--tyrosine, serine and cysteine--distinguishes it from all other cytosolic GSTs of known structure. Site-directed mutagenesis in combination with activity assays showed that instead of the classic catalytic residues, a water molecule stabilized by Ser129 and His123 acts as the deprotonator of the glutathione sulphur atom. Furthermore, only glycine and alanine are allowed at the amino-terminus of helix-alpha1 because of stereo-hindrance. Taken together, these results show that yeast Gtt2 is a novel atypical type of cytosolic GST.