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PDBsum entry 1gwc
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protein ligands Protein-protein interface(s) links
Transferase PDB id
1gwc

 

 

 

 

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Contents
Protein chains
221 a.a. *
Ligands
GTX ×3
SO4 ×3
Waters ×711
* Residue conservation analysis
PDB id:
1gwc
Name: Transferase
Title: The structure of a tau class glutathione s-transferase from wheat, active in herbicide detoxification
Structure: Glutathione s-transferase tsi-1. Chain: a, b, c. Synonym: tagstu4-4 glutathione s-transferase. Engineered: yes
Source: Aegilops tauschii. Bread wheat. Organism_taxid: 37682. Tissue: shoots. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Expression_system_variant: plyss. Other_details: wheat seedlings treated for 7 days with the wheat safener fenchlorazole-ethyl
Biol. unit: Monomer (from PDB file)
Resolution:
2.25Å     R-factor:   0.159     R-free:   0.211
Authors: R.Thom,I.Cummins,D.P.Dixon,R.Edwards,D.J.Cole,A.J.Lapthorn
Key ref:
R.Thom et al. (2002). Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification. Biochemistry, 41, 7008-7020. PubMed id: 12033934 DOI: 10.1021/bi015964x
Date:
14-Mar-02     Release date:   06-Jun-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
O04941  (O04941_AEGTA) -  glutathione transferase from Aegilops tauschii
Seq:
Struc: 		230 a.a.
221 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.18  - glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H+
RX
Bound ligand (Het Group name = GTX)
matches with 76.92% similarity 		+ glutathione
 = S-substituted glutathione
 + halide anion
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1021/bi015964x Biochemistry 41:7008-7020 (2002)
PubMed id: 12033934  
 
 
Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification.
R.Thom, I.Cummins, D.P.Dixon, R.Edwards, D.J.Cole, A.J.Lapthorn.
 
  ABSTRACT  
 
Glutathione S-transferases (GSTs) from the phi (GSTF) and tau (GSTU) classes are unique to plants and play important roles in stress tolerance and secondary metabolism as well as catalyzing the detoxification of herbicides in crops and weeds. We have cloned and functionally characterized a group of GSTUs from wheat treated with fenchlorazole-ethyl, a herbicide safener. One of these enzymes, TaGSTU4-4, was highly active in conjugating the chemically distinct wheat herbicides fenoxaprop and dimethenamid. The structure of TaGSTU4-4 has been determined at 2.2 A resolution in complex with S-hexylglutathione. This enzyme is the first tau class GST structure to be determined and most closely resembles the omega class GSTs, but without the unique N-terminal extension or active site cysteine. The X-ray structure identifies key amino acid residues in the hydrophobic binding site and provides insights into the substrate specificity of these enzymes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21428697 A.Oakley (2011).
Glutathione transferases: a structural perspective.
  Drug Metab Rev, 43, 138-151.  
21205172 C.L.Wang, and H.L.Yang (2011).
Conserved residues in the subunit interface of tau glutathione s-transferase affect catalytic and structural functions.
  J Integr Plant Biol, 53, 35-43.  
  21425939 I.Cummins, D.P.Dixon, S.Freitag-Pohl, M.Skipsey, and R.Edwards (2011).
Multiple roles for plant glutathione transferases in xenobiotic detoxification.
  Drug Metab Rev, 43, 266-280.  
19520850 D.P.Dixon, and R.Edwards (2009).
Selective binding of glutathione conjugates of Fatty Acid derivatives by plant glutathione transferases.
  J Biol Chem, 284, 21249-21256.  
18670133 Z.Li, X.Wang, J.Ma, G.Zhang, and Z.Ma (2008).
Cloning and characterization of a tau glutathione S-transferase subunit encoding gene in Gossypium hirsutum.
  Genes Genet Syst, 83, 219-225.  
17380533 Q.Zhang, F.Xu, K.N.Lambert, and D.E.Riechers (2007).
Safeners coordinately induce the expression of multiple proteins and MRP transcripts involved in herbicide metabolism and detoxification in Triticum tauschii seedling tissues.
  Proteomics, 7, 1261-1278.  
17173629 M.Skipsey, I.Cummins, C.J.Andrews, I.Jepson, and R.Edwards (2005).
Manipulation of plant tolerance to herbicides through co-ordinated metabolic engineering of a detoxifying glutathione transferase and thiol cosubstrate.
  Plant Biotechnol J, 3, 409-420.  
15906083 N.E.Labrou, M.Karavangeli, A.Tsaftaris, and Y.D.Clonis (2005).
Kinetic analysis of maize glutathione S-transferase I catalysing the detoxification from chloroacetanilide herbicides.
  Planta, 222, 91-97.  
15036861 E.Pechkova, and C.Nicolini (2004).
Protein nanocrystallography: a new approach to structural proteomics.
  Trends Biotechnol, 22, 117-122.  
15317585 G.A.Kotzia, and N.E.Labrou (2004).
S-(2,3-dichlorotriazinyl)glutathione. A new affinity label for probing the structure and function of glutathione transferases.
  Eur J Biochem, 271, 3503-3511.  
15037622 K.G.Kilili, N.Atanassova, A.Vardanyan, N.Clatot, K.Al-Sabarna, P.N.Kanellopoulos, A.M.Makris, and S.C.Kampranis (2004).
Differential roles of tau class glutathione S-transferases in oxidative stress.
  J Biol Chem, 279, 24540-24551.  
12692133 D.P.Dixon, A.G.McEwen, A.J.Lapthorn, and R.Edwards (2003).
Forced evolution of a herbicide detoxifying glutathione transferase.
  J Biol Chem, 278, 23930-23935.
PDB code: 1oyj
12587874 F.L.Theodoulou, I.M.Clark, X.L.He, K.E.Pallett, D.J.Cole, and D.L.Hallahan (2003).
Co-induction of glutathione-S-transferases and multidrug resistance associated protein by xenobiotics in wheat.
  Pest Manag Sci, 59, 202-214.  
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 code is shown on the right.

 

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