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PDBsum entry 1ags

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protein ligands links
Transferase (glutathione) PDB id
1ags
Jmol
Contents
Protein chain
221 a.a.* *
Ligands
GTX ×2
* Residue conservation analysis
* C-alpha coords only
PDB id:
1ags
Name: Transferase (glutathione)
Title: A surface mutant (g82r) of a human alpha-glutathione s- transferase shows decreased thermal stability and a new mode of molecular association in the crystal
Structure: Glutathione s-transferase alpha. Chain: a, b. Engineered: yes
Source: Synthetic construct. Organism_taxid: 32630. Organ: liver. Gene: pgth121-g82r. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.310    
Authors: K.Zeng,J.P.Rose,B.C.Wang
Key ref: K.Zeng et al. (1994). A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins, 20, 259-263. PubMed id: 7892174
Date:
23-Jan-95     Release date:   10-Jul-95    
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09210  (GSTA2_HUMAN) -  Glutathione S-transferase A2
Seq:
Struc:
222 a.a.
221 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 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 = GTX)
matches with 76.00% similarity
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     metabolic process   6 terms 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
Proteins 20:259-263 (1994)
PubMed id: 7892174  
 
 
A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.
K.Zeng, J.P.Rose, H.C.Chen, C.L.Strickland, C.P.Tu, B.C.Wang.
 
  ABSTRACT  
 
A chimeric enzyme (GST121) of the human alpha-glutathione S-transferases GST1-1 and GST2-2, which has improved catalytic efficiency and thermostability from its wild-type parent proteins, has been crystallized in a space group that is isomorphous with that reported for crystals of GST1-1. However, a single-site (G82R) mutant of GST121, which exhibits a significant reduction both in vitro and in vivo in protein thermostability, forms crystals that are not isomorphous with GST1-1. The mutant protein crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 49.5, b = 92.9, c = 115.9 A, and one dimer per asymmetric unit. Preliminary crystallographic results show that a mutation of the surface residue Gly 82 from a neutral to a charged residue causes new salt bridges to be formed among the GST dimers, suggesting that the G82R mutant might aggregate more readily than does GST121 in solution, resulting in a change of its solution properties.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
9188738 R.T.Koehler, H.O.Villar, K.E.Bauer, and D.L.Higgins (1997).
Ligand-based protein alignment and isozyme specificity of glutathione S-transferase inhibitors.
  Proteins, 28, 202-216.  
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.