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Transferase PDB id
Protein chains
213 a.a. *
ATA ×4
Waters ×48
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Glutathione s-transferase i from mais in complex with atrazine glutathione conjugate
Structure: Protein (glutathione s-transferase). Chain: a, b, c, d. Engineered: yes
Source: Zea mays. Organism_taxid: 4577. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
2.80Å     R-factor:   0.221     R-free:   0.305
Authors: L.Prade,R.Huber,B.Bieseler
Key ref:
L.Prade et al. (1998). Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants. Structure, 6, 1445-1452. PubMed id: 9817846 DOI: 10.1016/S0969-2126(98)00143-9
14-Oct-98     Release date:   21-Oct-98    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P12653  (GSTF1_MAIZE) -  Glutathione S-transferase 1
214 a.a.
213 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
Bound ligand (Het Group name = ATA)
matches with 60.00% 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  


DOI no: 10.1016/S0969-2126(98)00143-9 Structure 6:1445-1452 (1998)
PubMed id: 9817846  
Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants.
L.Prade, R.Huber, B.Bieseler.
BACKGROUND: Glutathione S-transferases (GSTs) are detoxifying enzymes present in all aerobic organisms. These enzymes catalyse the conjugation of glutathione with a variety of electrophilic compounds. In plants, GSTs catalyse the first step in the degradation of several herbicides, such as triazines and acetamides, thus playing an important role in herbicide tolerance. RESULTS: We have solved the structures of GST-I from maize in complex with an atrazine-glutathione conjugate (at 2.8 A resolution) and GST from Arabidopsis thaliana (araGST) in complex with an FOE-4053-glutathione conjugate (at 2.6 A resolution). These ligands are products of the detoxifying reaction and are well defined in the electron density. The herbicide-binding site (H site) is different in the two structures. The architecture of the glutathione-binding site (G site) of araGST is different to that of the previously described structure of GST in complex with two S-hexylglutathione molecules, but is homologous to that of GST-I. CONCLUSIONS: Three features are responsible for the differences in the H site of the two GSTs described here: the exchange of hydrophobic residues of different degrees of bulkiness; a slight difference in the location of the H site; and a difference in the degree of flexibility of the upper side of the H site, which is built up by the loop between helices alpha4 and alpha5. Taking these two structures as a model, the different substrate specificities of other plant GSTs may be explained. The structures reported here provide a basis for the design of new, more selective herbicides.
  Selected figure(s)  
Figure 5.
Figure 5. Overlay of the active sites of GST-I and araGST. The atrazine-GSH conjugate is shown in red and the FOE-4053-GSH conjugate is in green. Residues of the GST-I H site are in brown and those of araGST are in blue. The numbering is according to the GST-I sequence.
  The above figure is reprinted by permission from Cell Press: Structure (1998, 6, 1445-1452) copyright 1998.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  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.  
19016852 N.Allocati, L.Federici, M.Masulli, and C.Di Ilio (2009).
Glutathione transferases in bacteria.
  FEBS J, 276, 58-75.  
18691867 P.Kapoli, I.A.Axarli, D.Platis, M.Fragoulaki, M.Paine, J.Hemingway, J.Vontas, and N.E.Labrou (2008).
Engineering sensitive glutathione transferase for the detection of xenobiotics.
  Biosens Bioelectron, 24, 498-503.  
  18607078 H.Y.Cho, and K.H.Kong (2007).
Study on the biochemical characterization of herbicide detoxification enzyme, glutathione S-transferase.
  Biofactors, 30, 281-287.  
15309660 C.Raghavan, E.K.Ong, M.J.Dalling, and T.W.Stevenson (2005).
Effect of herbicidal application of 2,4-dichlorophenoxyacetic acid in Arabidopsis.
  Funct Integr Genomics, 5, 4.  
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.  
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.  
11453988 N.E.Labrou, L.V.Mello, and Y.D.Clonis (2001).
The conserved Asn49 of maize glutathione S-transferase I modulates substrate binding, catalysis and intersubunit communication.
  Eur J Biochem, 268, 3950-3957.  
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.