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PDBsum entry 1aw9

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protein metals links
Transferase PDB id
1aw9
Jmol
Contents
Protein chain
216 a.a. *
Metals
_CD ×5
Waters ×483
* Residue conservation analysis
PDB id:
1aw9
Name: Transferase
Title: Structure of glutathione s-transferase iii in apo form
Structure: Glutathione s-transferase iii. Chain: a. Engineered: yes. Other_details: apo form
Source: Zea mays. Organism_taxid: 4577. Variant: mutin. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
2.20Å     R-factor:   0.197    
Authors: T.Neuefeind,R.Huber,P.Reinemer,J.Knaeblein
Key ref:
T.Neuefeind et al. (1997). Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides. J Mol Biol, 274, 577-587. PubMed id: 9417936 DOI: 10.1006/jmbi.1997.1401
Date:
13-Oct-97     Release date:   28-Oct-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9ZP62  (Q9ZP62_MAIZE) -  Glutathione transferase III(A)
Seq:
Struc:
221 a.a.
216 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     response to toxin   2 terms 
  Biochemical function     transferase activity     2 terms  

 

 
DOI no: 10.1006/jmbi.1997.1401 J Mol Biol 274:577-587 (1997)
PubMed id: 9417936  
 
 
Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides.
T.Neuefeind, R.Huber, P.Reinemer, J.Knäblein, L.Prade, K.Mann, B.Bieseler.
 
  ABSTRACT  
 
Glutathione S-transferases (GSTs) are enzymes that inactivate toxic compounds by conjugation with glutathione and are involved in resistance towards drugs, antibiotics, insecticides and herbicides. Their ability to confer herbicide tolerance in plants provides a tool to control weeds in a wide variety of agronomic crops. GST-III was prepared from Zea mays var. mutin and its amino acid sequence was determined from two sets of peptides obtained by cleavage with endoprotease Asp-N and with trypsin, respectively. Recombinant GST-III was prepared by extraction of mRNA from plant tissue, transcription into cDNA, amplification by PCR and expression. It was crystallized and the crystal structure of the unligated form was determined at 2.2 A resolution. The enzyme forms a GST-typical dimer with one subunit consisting of 220 residues. Each subunit is formed of two distinct domains, an N-terminal domain consisting of a beta-sheet flanked by two helices, and a C-terminal domain, entirely helical. The dimeric molecule is globular with a large cleft between the two subunits. The amino acid sequence of GST-III and its cDNA sequence determined here show differences from sequences published earlier.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Stereo ribbon representation of a dimer of GST-III viewed perpendicular the 2-fold symmetry axis. The Figure was made with RASTER3D [Merrit and Murphy 1994].
Figure 6.
Figure 6. Molecular surface viewed along the 2-fold symmetry axis, showing the large cavity formed between the subunits.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 274, 577-587) copyright 1997.  
  Figures were 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.  
20143451 A.J.Salazar-Medina, L.García-Rico, K.D.García-Orozco, E.Valenzuela-Soto, C.A.Contreras-Vergara, R.Arreola, A.Arvizu-Flores, and R.R.Sotelo-Mundo (2010).
Inhibition by Cu2+ and Cd2+ of a mu-class glutathione S-transferase from shrimp Litopenaeus vannamei.
  J Biochem Mol Toxicol, 24, 218-222.  
20135200 S.Banerjee, and R.Goswami (2010).
GST profile expression study in some selected plants: in silico approach.
  Mol Cell Biochem, 336, 109-126.  
18820023 Y.Huang, R.Xun, G.Chen, and L.Xun (2008).
Maintenance role of a glutathionyl-hydroquinone lyase (PcpF) in pentachlorophenol degradation by Sphingobium chlorophenolicum ATCC 39723.
  J Bacteriol, 190, 7595-7600.  
17682821 B.Blanchette, X.Feng, and B.R.Singh (2007).
Marine glutathione S-transferases.
  Mar Biotechnol (NY), 9, 513-542.  
12972411 M.Perbandt, C.Burmeister, R.D.Walter, C.Betzel, and E.Liebau (2004).
Native and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum.
  J Biol Chem, 279, 1336-1342.
PDB codes: 1pa3 1q4j
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
  11897031 D.P.Dixon, A.Lapthorn, and R.Edwards (2002).
Plant glutathione transferases.
  Genome Biol, 3, REVIEWS3004.  
12207667 M.W.Bianchi, C.Roux, and N.Vartanian (2002).
Drought regulation of GST8, encoding the Arabidopsis homologue of ParC/Nt107 glutathione transferase/peroxidase.
  Physiol Plant, 116, 96.  
11604524 A.J.Oakley, T.Harnnoi, R.Udomsinprasert, K.Jirajaroenrat, A.J.Ketterman, and M.C.Wilce (2001).
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.
  Protein Sci, 10, 2176-2185.
PDB codes: 1jlv 1jlw
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.  
11093265 W.S.Valdar, and J.M.Thornton (2001).
Protein-protein interfaces: analysis of amino acid conservation in homodimers.
  Proteins, 42, 108-124.  
  10548067 J.U.Flanagan, J.Rossjohn, M.W.Parker, P.G.Board, and G.Chelvanayagam (1999).
Mutagenic analysis of conserved arginine residues in and around the novel sulfate binding pocket of the human Theta class glutathione transferase T2-2.
  Protein Sci, 8, 2205-2212.  
9665696 A.J.Oakley, M.Lo Bello, G.Ricci, G.Federici, and M.W.Parker (1998).
Evidence for an induced-fit mechanism operating in pi class glutathione transferases.
  Biochemistry, 37, 9912-9917.
PDB codes: 14gs 16gs
10066594 D.P.Dixon, L.Cummins, D.J.Cole, and R.Edwards (1998).
Glutathione-mediated detoxification systems in plants.
  Curr Opin Plant Biol, 1, 258-266.  
9829702 J.U.Flanagan, J.Rossjohn, M.W.Parker, P.G.Board, and G.Chelvanayagam (1998).
A homology model for the human theta-class glutathione transferase T1-1.
  Proteins, 33, 444-454.  
9817846 L.Prade, R.Huber, and B.Bieseler (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.
PDB codes: 1bx9 1bye
9818188 R.N.Armstrong (1998).
Mechanistic imperatives for the evolution of glutathione transferases.
  Curr Opin Chem Biol, 2, 618-623.  
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.