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PDBsum entry 3rpp

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protein Protein-protein interface(s) links
Transferase PDB id
3rpp
Jmol
Contents
Protein chain
216 a.a.
Waters ×752
PDB id:
3rpp
Name: Transferase
Title: Crystal structure of human kappa class glutathione transfera form
Structure: Glutathione s-transferase kappa 1. Chain: a, b, c. Synonym: gst 13-13, gst class-kappa, gstk1-1, hgstk1, gluta transferase subunit 13. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstk1, hdcmd47p. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.154     R-free:   0.195
Authors: B.Wang,Y.Peng,T.Zhang,J.Ding
Key ref: B.Wang et al. (2011). Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism. Biochem J, 439, 215-225. PubMed id: 21728995 DOI: 10.1042/BJ20110753
Date:
27-Apr-11     Release date:   13-Jul-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y2Q3  (GSTK1_HUMAN) -  Glutathione S-transferase kappa 1
Seq:
Struc:
226 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
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   7 terms 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     transferase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1042/BJ20110753 Biochem J 439:215-225 (2011)
PubMed id: 21728995  
 
 
Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism.
B.Wang, Y.Peng, T.Zhang, J.Ding.
 
  ABSTRACT  
 
GSTs (glutathione transferases) are a family of enzymes that primarily catalyse nucleophilic addition of the thiol of GSH (reduced glutathione) to a variety of hydrophobic electrophiles in the cellular detoxification of cytotoxic and genotoxic compounds. GSTks (Kappa class GSTs) are a distinct class because of their unique cellular localization, function and structure. In the present paper we report the crystal structures of hGSTk (human GSTk) in apo-form and in complex with GTX (S-hexylglutathione) and steady-state kinetic studies, revealing insights into the catalytic mechanism of hGSTk and other GSTks. Substrate binding induces a conformational change of the active site from an 'open' conformation in the apo-form to a 'closed' conformation in the GTX-bound complex, facilitating formations of the G site (GSH-binding site) and the H site (hydrophobic substrate-binding site). The conserved Ser(16) at the G site functions as the catalytic residue in the deprotonation of the thiol group and the conserved Asp(69), Ser(200), Asp(201) and Arg(202) form a network of interactions with γ-glutamyl carboxylate to stabilize the thiolate anion. The H site is a large hydrophobic pocket with conformational flexibility to allow the binding of different hydrophobic substrates. The kinetic mechanism of hGSTk conforms to a rapid equilibrium random sequential Bi Bi model.