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PDBsum entry 1u88

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1u88
Jmol
Contents
Protein chains
209 a.a. *
Ligands
GTY
* Residue conservation analysis
PDB id:
1u88
Name: Transferase
Title: Crystal structure of the 26 kda glutathione s-transferase y7f mutant from schistosoma japonicum complexed with s- octyl glutathione
Structure: Glutathione s-transferase 26 kda. Chain: a, b. Synonym: glutathione s-transferase. Engineered: yes. Mutation: yes
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
3.50Å     R-factor:   0.220     R-free:   0.317
Authors: A.W.Smith,A.Camara-Artigas
Key ref:
M.Andújar-Sánchez et al. (2005). Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum. Biochemistry, 44, 1174-1183. PubMed id: 15667211 DOI: 10.1021/bi0483110
Date:
05-Aug-04     Release date:   22-Feb-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08515  (GST26_SCHJA) -  Glutathione S-transferase class-mu 26 kDa isozyme
Seq:
Struc:
218 a.a.
209 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.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+
glutathione
Bound ligand (Het Group name = GTY)
matches with 71.00% similarity
= 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/bi0483110 Biochemistry 44:1174-1183 (2005)
PubMed id: 15667211  
 
 
Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.
M.Andújar-Sánchez, A.W.Smith, J.M.Clemente-Jimenez, F.Rodriguez-Vico, F.J.Las Heras-Vazquez, V.Jara-Pérez, A.Cámara-Artigas.
 
  ABSTRACT  
 
Glutathione S-transferases are a family of multifunctional enzymes involved in the metabolism of drugs and xenobiotics. Two tyrosine residues, Tyr 7 and Tyr 111, in the active site of the enzyme play an important role in the binding and catalysis of substrate ligands. The crystal structures of Schistosoma japonicum glutathione S-transferase tyrosine 7 to phenylalanine mutant [SjGST(Y7F)] in complex with the substrate glutathione (GSH) and the competitive inhibitor S-octylglutathione (S-octyl-GSH) have been obtained. These new structural data combined with fluorescence spectroscopy and thermodynamic data, obtained by means of isothermal titration calorimetry, allow for detailed characterization of the ligand-binding process. The binding of S-octyl-GSH to SjGST(Y7F) is enthalpically and entropically driven at temperatures below 30 degrees C. The stoichiometry of the binding is one molecule of S-octyl-GSH per mutant dimer, whereas shorter alkyl derivatives bind with a stoichiometry of two molecules per mutant dimer. The SjGST(Y7F).GSH structure showed no major structural differences compared to the wild-type enzyme. In contrast, the structure of SjGST(Y7F).S-octyl-GSH showed asymmetric binding of S-octyl-GSH. This lack of symmetry is reflected in the lower symmetry space group of the SjGST(Y7F).S-octyl-GSH crystals (P6(3)) compared to that of the SjGST(Y7F).GSH crystals (P6(3)22). Moreover, the binding of S-octyl-GSH to the A subunit is accompanied by conformational changes that may be responsible for the lack of binding to the B subunit.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20489719 V.T.Bhat, A.M.Caniard, T.Luksch, R.Brenk, D.J.Campopiano, and M.F.Greaney (2010).
Nucleophilic catalysis of acylhydrazone equilibration for protein-directed dynamic covalent chemistry.
  Nat Chem, 2, 490-497.  
  19177365 M.Sagermann, R.R.Chapleau, E.DeLorimier, and M.Lei (2009).
Using affinity chromatography to engineer and characterize pH-dependent protein switches.
  Protein Sci, 18, 217-228.
PDB codes: 3crt 3cru 3d0z
17006876 A.Ababou, and J.E.Ladbury (2007).
Survey of the year 2005: literature on applications of isothermal titration calorimetry.
  J Mol Recognit, 20, 4.  
16552148 A.Palencia, J.C.Martinez, P.L.Mateo, I.Luque, and A.Camara-Artigas (2006).
Structure of human TSG101 UEV domain.
  Acta Crystallogr D Biol Crystallogr, 62, 458-464.
PDB code: 2f0r
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.