PDBsum entry 1eoh

Go to PDB code: 
protein Protein-protein interface(s) links
Transferase PDB id
Protein chain
(+ 2 more) 209 a.a. *
Waters ×500
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Glutathione transferase p1-1
Structure: Glutathione s-transferase. Chain: a, b, c, d, e, f, g, h. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_organ: liver.
Biol. unit: Dimer (from PQS)
2.50Å     R-factor:   0.231     R-free:   0.286
Authors: J.Rossjohn,W.J.Mckinstry,A.J.Oakley,M.W.Parker,G.Stenberg, B.Mannervik,B.Dragani,R.Cocco,A.Aceto
Key ref:
J.Rossjohn et al. (2000). Structures of thermolabile mutants of human glutathione transferase P1-1. J Mol Biol, 302, 295-302. PubMed id: 10970734 DOI: 10.1006/jmbi.2000.4054
22-Mar-00     Release date:   18-Oct-00    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P09211  (GSTP1_HUMAN) -  Glutathione S-transferase P
210 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.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
+ 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     TRAF2-GSTP1 complex   10 terms 
  Biological process     metabolic process   31 terms 
  Biochemical function     S-nitrosoglutathione binding     8 terms  


DOI no: 10.1006/jmbi.2000.4054 J Mol Biol 302:295-302 (2000)
PubMed id: 10970734  
Structures of thermolabile mutants of human glutathione transferase P1-1.
J.Rossjohn, W.J.McKinstry, A.J.Oakley, M.W.Parker, G.Stenberg, B.Mannervik, B.Dragani, R.Cocco, A.Aceto.
An N-capping box motif (Ser/Thr-Xaa-Xaa-Asp) is strictly conserved at the beginning of helix alpha6 in the core of virtually all glutathione transferases (GST) and GST-related proteins. It has been demonstrated that this local motif is important in determining the alpha-helical propensity of the isolated alpha6-peptide and plays a crucial role in the folding and stability of GSTs. Its removal by site-directed mutagenesis generated temperature-sensitive folding mutants unable to refold at physiological temperature (37 degrees C). In the present work, variants of human GSTP1-1 (S150A and D153A), in which the capping residues have been substituted by alanine, have been generated and purified for structural analysis. Thus, for the first time, temperature-sensitive folding mutants of an enzyme, expressed at a permissive temperature, have been crystallized and their three-dimensional structures determined by X-ray crystallography. The crystal structures of human pi class GST temperature-sensitive mutants provide a basis for understanding the structural origin of the dramatic effects observed on the overall stability of the enzyme at higher temperatures upon single substitution of a capping residue.
  Selected figure(s)  
Figure 1.
Figure 1. Ribbon picture of a monomer of human pi class GST. The location of helix a6, the GST motif II (the conserved sequence motif consisting of helix a6 and the preceding long loop), GSH and the sites of mutation (shown in ball-and-stick) are indicated. This Figure was produced using MOLSCRIPT [Kraulis 1991].
Figure 2.
Figure 2. Stereoviews of the region in GST P1-1 about the sites of mutation. The N-terminal end of helix a6 is shown in ribbon representation and key residues are shown as ball-and-stick. (a) Wild-type structure (9GSS; [Oakley et al 1997]), (b) S150A and (c) D153A. The Figure was produced using MOLSCRIPT [Kraulis 1991].
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 302, 295-302) copyright 2000.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16012173 P.Winayanuwattikun, and A.J.Ketterman (2005).
An electron-sharing network involved in the catalytic mechanism is functionally conserved in different glutathione transferase classes.
  J Biol Chem, 280, 31776-31782.  
12414796 G.K.Kong, G.Polekhina, W.J.McKinstry, M.W.Parker, B.Dragani, A.Aceto, D.Paludi, D.R.Principe, B.Mannervik, and G.Stenberg (2003).
Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1.
  J Biol Chem, 278, 1291-1302.
PDB codes: 1md3 1md4
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.