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PDBsum entry 1guk

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protein Protein-protein interface(s) links
Transferase PDB id
1guk
Jmol
Contents
Protein chains
215 a.a. *
* Residue conservation analysis
PDB id:
1guk
Name: Transferase
Title: Crystal structure of murine alpha-class gsta4-4
Structure: Glutathione s-transferase a4-4. Chain: a, b. Synonym: mgsta4-4, gst5.7. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: lung. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
2.90Å     R-factor:   0.234    
Authors: U.Krengel,K.H.Schroter,H.Hoier,B.W.Dijkstra
Key ref:
U.Krengel et al. (1998). Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress. FEBS Lett, 422, 285-290. PubMed id: 9498801 DOI: 10.1016/S0014-5793(98)00026-X
Date:
11-Dec-97     Release date:   08-Apr-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P24472  (GSTA4_MOUSE) -  Glutathione S-transferase A4
Seq:
Struc:
222 a.a.
215 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
= 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   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0014-5793(98)00026-X FEBS Lett 422:285-290 (1998)
PubMed id: 9498801  
 
 
Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress.
U.Krengel, K.H.Schröter, H.Hoier, A.Arkema, K.H.Kalk, P.Zimniak, B.W.Dijkstra.
 
  ABSTRACT  
 
Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification. The enzymes protect the cells against toxicants by conjugating them to glutathione. Recently, a novel subgroup of alpha-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress. Here, we report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup. The structure was solved by molecular replacement and refined to 2.9 A resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Ramachandran plot as obtained from PROCHECK [41]. Val-174 of molecule A (named 1174) has unfavorable ,ψ angles. However, its conformation is well supported by electron density (real space correlation coefficient of OMIT map is 0.81).
Figure 3.
Fig. 3. A: Stereo view of the overall structure of one subunit of mGSTA4-4. Domain 1 and 2, the N- and C-terminus as well as helices 4, 5′ and 9 have been labelled. B: Stereo view of the substrate binding site of mGSTA4-4 (dark lines) compared to hGSTA1-1 (PDB ID code 1GUH) (light line). Both figures were prepared with Molscript [42].
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (1998, 422, 285-290) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
15789344 J.An, Q.Yuan, C.Wang, L.Liu, K.Tang, H.Y.Tian, N.H.Jing, and F.K.Zhao (2005).
Differential display of proteins involved in the neural differentiation of mouse embryonic carcinoma P19 cells by comparative proteomic analysis.
  Proteomics, 5, 1656-1668.  
14690442 S.Mosebi, Y.Sayed, J.Burke, and H.W.Dirr (2003).
Residue 219 impacts on the dynamics of the C-terminal region in glutathione transferase A1-1: implications for stability and catalytic and ligandin functions.
  Biochemistry, 42, 15326-15332.  
11119643 E.T.Adman, I.Le Trong, R.E.Stenkamp, B.S.Nieslanik, E.C.Dietze, G.Tai, C.Ibarra, and W.M.Atkins (2001).
Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y.
  Proteins, 42, 192-200.
PDB codes: 1ev4 1ev9
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