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PDBsum entry 1gss
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Transferase/transferase inhibitor PDB id
1gss

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
209 a.a. *
Ligands
LEE ×2
Waters ×205
* Residue conservation analysis
PDB id:
1gss
Name: Transferase/transferase inhibitor
Title: Three-dimensional structure of class pi glutathione s-transferase from human placenta in complex with s-hexylglutathione at 2.8 angstroms resolution
Structure: Glutathione s-transferase. Chain: a, b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: placenta
Biol. unit: Dimer (from PQS)
Resolution:
2.80Å     R-factor:   0.196    
Authors: P.Reinemer,H.W.Dirr,R.Ladenstein,M.Lobello,G.Federici,R.Huber, M.W.Parker
Key ref:
P.Reinemer et al. (1992). Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol, 227, 214-226. PubMed id: 1522586 DOI: 10.1016/0022-2836(92)90692-D
Date:
28-May-92     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09211  (GSTP1_HUMAN) -  Glutathione S-transferase P from Homo sapiens
Seq:
Struc: 		210 a.a.
209 a.a.
Key:    PfamA domain  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 = LEE)
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: 10.1016/0022-2836(92)90692-D J Mol Biol 227:214-226 (1992)
PubMed id: 1522586  
 
 
Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.
P.Reinemer, H.W.Dirr, R.Ladenstein, R.Huber, M.Lo Bello, G.Federici, M.W.Parker.
 
  ABSTRACT  
 
The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure.
 
  Selected figure(s)  
 
Figure 8.
Figure 8. Conolly dot surface of the op region of human class x glutathione S-transferase showing both active sites occupied by S-hexyllutathione. View is along the local dyad. Also shown is the cavity formed between the 2 subunits. 		Figure 9.
Figure 9. Model o inhibitor S-hexylglutathione and its next neighbors at the active site of human -transferase.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1992, 227, 214-226) copyright 1992.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21323601 A.J.Ketterman, C.Saisawang, and J.Wongsantichon (2011).
Insect glutathione transferases.
  Drug Metab Rev, 43, 253-265.  
  21428697 A.Oakley (2011).
Glutathione transferases: a structural perspective.
  Drug Metab Rev, 43, 138-151.  
20540076 I.Quesada-Soriano, L.J.Parker, A.Primavera, J.Wielens, J.K.Holien, J.M.Casas-Solvas, A.Vargas-Berenguel, A.M.Aguilera, M.Nuccetelli, A.P.Mazzetti, M.L.Bello, M.W.Parker, and L.García-Fuentes (2011).
Diuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108V.
  J Mol Recognit, 24, 220-234.
PDB codes: 3km6 3kmo
  21351850 K.D.Tew, and D.M.Townsend (2011).
Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification.
  Drug Metab Rev, 43, 179-193.  
19780048 I.Quesada-Soriano, L.J.Parker, A.Primavera, J.M.Casas-Solvas, A.Vargas-Berenguel, C.Barón, C.J.Morton, A.Paola Mazzetti, M.Lo Bello, M.W.Parker, and L.García-Fuentes (2009).
Influence of the H-site residue 108 on human glutathione transferase P1-1 ligand binding: Structure-thermodynamic relationships and thermal stability.
  Protein Sci, 18, 2454-2470.
PDB codes: 3hjm 3hjo 3hkr
18424441 L.M.Balogh, A.G.Roberts, L.M.Shireman, R.J.Greene, and W.M.Atkins (2008).
The stereochemical course of 4-hydroxy-2-nonenal metabolism by glutathione S-transferases.
  J Biol Chem, 283, 16702-16710.  
18796433 Y.C.Huang, S.Misquitta, S.Y.Blond, E.Adams, and R.F.Colman (2008).
Catalytically Active Monomer of Glutathione S-Transferase {pi} and Key Residues Involved in the Electrostatic Interaction between Subunits.
  J Biol Chem, 283, 32880-32888.  
17682821 B.Blanchette, X.Feng, and B.R.Singh (2007).
Marine glutathione S-transferases.
  Mar Biotechnol (NY), 9, 513-542.  
17587159 Y.Wu, J.Shen, and Z.Yin (2007).
Expression, purification and functional analysis of hexahistidine-tagged human glutathione S-transferase P1-1 and its cysteinyl mutants.
  Protein J, 26, 359-370.  
16342067 C.Lu, M.R.Spitz, H.Zhao, Q.Dong, M.Truong, J.Y.Chang, G.R.Blumenschein, W.K.Hong, and X.Wu (2006).
Association between glutathione S-transferase pi polymorphisms and survival in patients with advanced nonsmall cell lung carcinoma.
  Cancer, 106, 441-447.  
16597834 R.Téllez-Sanz, E.Cesareo, M.Nuccetelli, A.M.Aguilera, C.Barón, L.J.Parker, J.J.Adams, C.J.Morton, M.Lo Bello, M.W.Parker, and L.García-Fuentes (2006).
Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1.
  Protein Sci, 15, 1093-1105.
PDB codes: 2a2r 2a2s
16788955 W.Q.Liao, X.F.Liang, L.Wang, L.M.Lei, and B.P.Han (2006).
Molecular cloning and characterization of alpha-class glutathione S-transferase gene from the liver of silver carp, bighead carp, and other major Chinese freshwater fishes.
  J Biochem Mol Toxicol, 20, 114-126.  
16143001 J.M.Allan, and C.S.Rabkin (2005).
Genetic susceptibility to iatrogenic malignancy.
  Pharmacogenomics, 6, 615-628.  
16050796 K.D.Tew (2005).
TLK-286: a novel glutathione S-transferase-activated prodrug.
  Expert Opin Investig Drugs, 14, 1047-1054.  
15640152 M.Perbandt, J.Höppner, C.Betzel, R.D.Walter, and E.Liebau (2005).
Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.
  J Biol Chem, 280, 12630-12636.
PDB codes: 1tu7 1tu8
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
14676193 U.M.Hegazy, B.Mannervik, and G.Stenberg (2004).
Functional role of the lock and key motif at the subunit interface of glutathione transferase p1-1.
  J Biol Chem, 279, 9586-9596.  
12937169 E.Ortiz-Salmerón, M.Nuccetelli, A.J.Oakley, M.W.Parker, M.Lo Bello, and L.García-Fuentes (2003).
Thermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathione.
  J Biol Chem, 278, 46938-46948.
PDB code: 22gs
12972429 M.G.Jeppesen, P.Ortiz, W.Shepard, T.G.Kinzy, J.Nyborg, and G.R.Andersen (2003).
The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae.
  J Biol Chem, 278, 47190-47198.
PDB code: 1nhy
12127579 T.Bucciarelli, P.Sacchetta, F.Amicarelli, R.Petruzzelli, S.Melino, D.Rotilio, N.Celli, and C.Di Ilio (2002).
Amino acid sequence of the major form of toad liver glutathione transferase.
  Int J Biochem Cell Biol, 34, 1286-1290.  
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
11327815 G.Polekhina, P.G.Board, A.C.Blackburn, and M.W.Parker (2001).
Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity.
  Biochemistry, 40, 1567-1576.
PDB code: 1fw1
11294649 M.Chang, Y.G.Shin, R.B.van Breemen, S.Y.Blond, and J.L.Bolton (2001).
Structural and functional consequences of inactivation of human glutathione S-transferase P1-1 mediated by the catechol metabolite of equine estrogens, 4-hydroxyequilenin.
  Biochemistry, 40, 4811-4820.  
11447114 T.L.Ung, C.Cao, J.Lu, K.Ozato, and T.E.Dever (2001).
Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.
  EMBO J, 20, 3728-3737.  
11123923 C.Micaloni, A.P.Mazzetti, M.Nuccetelli, J.Rossjohn, W.J.McKinstry, G.Antonini, A.M.Caccuri, A.J.Oakley, G.Federici, G.Ricci, M.W.Parker, and M.Lo Bello (2000).
Valine 10 may act as a driver for product release from the active site of human glutathione transferase P1-1.
  Biochemistry, 39, 15961-15970.  
10858281 S.A.McCallum, T.K.Hitchens, C.Torborg, and G.S.Rule (2000).
Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase.
  Biochemistry, 39, 7343-7356.  
10383436 A.M.Caccuri, G.Antonini, P.Ascenzi, M.Nicotra, M.Nuccetelli, A.P.Mazzetti, G.Federici, M.Lo Bello, and G.Ricci (1999).
Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding.
  J Biol Chem, 274, 19276-19280.  
  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.  
10559245 L.Tang, B.Guo, A.Javed, J.Y.Choi, S.Hiebert, J.B.Lian, A.J.van Wijnen, J.L.Stein, G.S.Stein, and G.W.Zhou (1999).
Crystal structure of the nuclear matrix targeting signal of the transcription factor acute myelogenous leukemia-1/polyoma enhancer-binding protein 2alphaB/core binding factor alpha2.
  J Biol Chem, 274, 33580-33586.  
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
9551553 J.Rossjohn, W.J.McKinstry, A.J.Oakley, D.Verger, J.Flanagan, G.Chelvanayagam, K.L.Tan, P.G.Board, and M.W.Parker (1998).
Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.
  Structure, 6, 309-322.
PDB codes: 1ljr 2ljr 3ljr
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.  
9722558 L.Stella, A.M.Caccuri, N.Rosato, M.Nicotra, M.Lo Bello, F.De Matteis, A.P.Mazzetti, G.Federici, and G.Ricci (1998).
Flexibility of helix 2 in the human glutathione transferase P1-1. time-resolved fluorescence spectroscopy.
  J Biol Chem, 273, 23267-23273.  
9446594 M.C.Vega, S.B.Walsh, T.J.Mantle, and M.Coll (1998).
The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region.
  J Biol Chem, 273, 2844-2850.
PDB codes: 1bay 1gti
9485454 M.Nicotra, M.Paci, M.Sette, A.J.Oakley, M.W.Parker, M.Lo Bello, A.M.Caccuri, G.Federici, and G.Ricci (1998).
Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure.
  Biochemistry, 37, 3020-3027.  
9761841 W.J.McKinstry, A.J.Oakley, J.Rossjohn, D.Verger, K.L.Tan, P.G.Board, and M.W.Parker (1998).
Preliminary X-ray crystallographic studies of a newly defined human theta-class glutathione transferase.
  Acta Crystallogr D Biol Crystallogr, 54, 148-150.  
9012673 A.J.Oakley, J.Rossjohn, M.Lo Bello, A.M.Caccuri, G.Federici, and M.W.Parker (1997).
The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate.
  Biochemistry, 36, 576-585.
PDB codes: 2gss 3gss
9183003 G.Antonini, G.Pitari, A.M.Caccuri, G.Ricci, D.Boschi, R.Fruttero, A.Gasco, and P.Ascenzi (1997).
Inhibition of human placenta glutathione transferase P1-1 by the antibiotic calvatic acid and its diazocyanide analogue--evidence for multiple catalytic intermediates.
  Eur J Biochem, 245, 663-667.  
9037717 G.Chelvanayagam, M.C.Wilce, M.W.Parker, K.L.Tan, and P.G.Board (1997).
Homology model for the human GSTT2 Theta class glutathione transferase.
  Proteins, 27, 118-130.  
10837536 K.D.Tew, S.Dutta, and M.Schultz (1997).
Inhibitors of glutathione S-transferases as therapeutic agents.
  Adv Drug Deliv Rev, 26, 91.  
  9007975 L.Hu, B.L.Borleske, and R.F.Colman (1997).
Probing the active site of alpha-class rat liver glutathione S-transferases using affinity labeling by monobromobimane.
  Protein Sci, 6, 43-52.  
9351803 L.Prade, R.Huber, T.H.Manoharan, W.E.Fahl, and W.Reuter (1997).
Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor.
  Structure, 5, 1287-1295.
PDB codes: 1aqv 1aqw 1aqx
9407009 M.J.Snyder, and D.R.Maddison (1997).
Molecular phylogeny of glutathione-S-transferases.
  DNA Cell Biol, 16, 1373-1384.  
9166793 M.Lo Bello, A.J.Oakley, A.Battistoni, A.P.Mazzetti, M.Nuccetelli, G.Mazzarese, J.Rossjohn, M.W.Parker, and G.Ricci (1997).
Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme.
  Biochemistry, 36, 6207-6217.
PDB code: 4gss
9188738 R.T.Koehler, H.O.Villar, K.E.Bauer, and D.L.Higgins (1997).
Ligand-based protein alignment and isozyme specificity of glutathione S-transferase inhibitors.
  Proteins, 28, 202-216.  
9245401 X.Ji, M.Tordova, R.O'Donnell, J.F.Parsons, J.B.Hayden, G.L.Gilliland, and P.Zimniak (1997).
Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase.
  Biochemistry, 36, 9690-9702.
PDB codes: 1pgt 2pgt
8663073 A.M.Caccuri, P.Ascenzi, G.Antonini, M.W.Parker, A.J.Oakley, E.Chiessi, M.Nuccetelli, A.Battistoni, A.Bellizia, and G.Ricci (1996).
Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor co-substrate on dynamics and kinetics of human glutathione transferase.
  J Biol Chem, 271, 16193-16198.  
8807865 E.W.Napolitano, H.O.Villar, L.M.Kauvar, D.L.Higgins, D.Roberts, J.Mandac, S.K.Lee, A.Engqvist-Goldstein, R.Bukar, B.L.Calio, H.M.Jäck, and J.A.Tainer (1996).
Glubodies: randomized libraries of glutathione transferase enzymes.
  Chem Biol, 3, 359-367.  
8663072 G.Ricci, A.M.Caccuri, M.Lo Bello, N.Rosato, G.Mei, M.Nicotra, E.Chiessi, A.P.Mazzetti, and G.Federici (1996).
Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism.
  J Biol Chem, 271, 16187-16192.  
8664265 G.Xiao, S.Liu, X.Ji, W.W.Johnson, J.Chen, J.F.Parsons, W.J.Stevens, G.L.Gilliland, and R.N.Armstrong (1996).
First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase.
  Biochemistry, 35, 4753-4765.
PDB codes: 6gst 6gsu 6gsv 6gsw 6gsx 6gsy
8643551 H.W.Sun, J.Bernhagen, R.Bucala, and E.Lolis (1996).
Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor.
  Proc Natl Acad Sci U S A, 93, 5191-5196.
PDB code: 1mif
  8762135 J.Wang, J.J.Barycki, and R.F.Colman (1996).
Tyrosine 8 contributes to catalysis but is not required for activity of rat liver glutathione S-transferase, 1-1.
  Protein Sci, 5, 1032-1042.  
8672473 M.Widersten, R.Björnestedt, and B.Mannervik (1996).
Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1.
  Biochemistry, 35, 7731-7742.  
8917446 N.Sluis-Cremer, N.N.Naidoo, W.H.Kaplan, T.H.Manoharan, W.E.Fahl, and H.W.Dirr (1996).
Determination of a binding site for a non-substrate ligand in mammalian cytosolic glutathione S-transferases by means of fluorescence-resonance energy transfer.
  Eur J Biochem, 241, 484-488.  
8973647 N.Sluis-Cremer, N.Naidoo, and H.Dirr (1996).
Class-pi glutathione S-transferase is unable to regain its native conformation after oxidative inactivation by hydrogen peroxide.
  Eur J Biochem, 242, 301-307.  
8694853 R.Whalen, E.S.Kempner, and T.D.Boyer (1996).
Structural studies of a human pi class glutathione S-transferase. Photoaffinity labeling of the active site and target size analysis.
  Biochem Pharmacol, 52, 281-288.  
8910329 T.E.McHugh, W.M.Atkins, J.K.Racha, K.L.Kunze, and D.L.Eaton (1996).
Binding of the aflatoxin-glutathione conjugate to mouse glutathione S-transferase A3-3 is saturated at only one ligand per dimer.
  J Biol Chem, 271, 27470-27474.  
8710848 X.Ji, E.C.von Rosenvinge, W.W.Johnson, R.N.Armstrong, and G.L.Gilliland (1996).
Location of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallography.
  Proc Natl Acad Sci U S A, 93, 8208-8213.
PDB code: 2gsq
7496993 A.Aceto, B.Dragani, N.Allocati, S.Angelucci, T.Bucciarelli, P.Sacchetta, C.D.Di Ilio, and F.Martini (1995).
Analysis by limited proteolysis of domain organization and GSH-site arrangement of bacterial glutathione transferase B1-1.
  Int J Biochem Cell Biol, 27, 1033-1041.  
8591048 A.D.Cameron, I.Sinning, G.L'Hermite, B.Olin, P.G.Board, B.Mannervik, and T.A.Jones (1995).
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate.
  Structure, 3, 717-727.
PDB codes: 1gsd 1gse 1gsf
7667259 A.M.Gulick, and W.E.Fahl (1995).
Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme.
  Proc Natl Acad Sci U S A, 92, 8140-8144.  
7667397 A.M.Gulick, and W.E.Fahl (1995).
Mammalian glutathione S-transferase: regulation of an enzyme system to achieve chemotherapeutic efficacy.
  Pharmacol Ther, 66, 237-257.  
7836386 G.Ricci, M.Lo Bello, A.M.Caccurri, A.Pastore, M.Nuccetelli, M.W.Parker, and G.Federici (1995).
Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperatively in glutathione transferase P1-1.
  J Biol Chem, 270, 1243-1248.  
7814427 H.C.Lee, Y.P.Toung, Y.S.Tu, and C.P.Tu (1995).
A molecular genetic approach for the identification of essential residues in human glutathione S-transferase function in Escherichia coli.
  J Biol Chem, 270, 99.  
7607236 J.Erhardt, and H.Dirr (1995).
Native dimer stabilizes the subunit tertiary structure of porcine class pi glutathione S-transferase.
  Eur J Biochem, 230, 614-620.  
7788290 J.L.Martin (1995).
Thioredoxin--a fold for all reasons.
  Structure, 3, 245-250.  
7556138 J.Nishihira, M.Sakai, S.Nishi, and Y.Hatanaka (1995).
Identification of the electrophilic substrate-binding site of glutathione S-transferase P by photoaffinity labeling.
  Eur J Biochem, 232, 106-110.  
7665611 L.Hu, and R.F.Colman (1995).
Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3.
  J Biol Chem, 270, 21875-21883.  
  7774571 M.C.Wilce, P.G.Board, S.C.Feil, and M.W.Parker (1995).
Crystal structure of a theta-class glutathione transferase.
  EMBO J, 14, 2133-2143.  
7836387 M.Lo Bello, A.Battistoni, A.P.Mazzetti, P.G.Board, M.Muramatsu, G.Federici, and G.Ricci (1995).
Site-directed mutagenesis of human glutathione transferase P1-1. Spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants.
  J Biol Chem, 270, 1249-1253.  
  8770367 M.W.Parker (1995).
Protein crystallography in Australia.
  Aust N Z J Med, 25, 876-882.  
7696312 P.Bico, J.Erhardt, W.Kaplan, and H.Dirr (1995).
Porcine class pi glutathione S-transferase: anionic ligand binding and conformational analysis.
  Biochim Biophys Acta, 1247, 225-230.  
8530359 R.Björnestedt, S.Tardioli, and B.Mannervik (1995).
The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site.
  J Biol Chem, 270, 29705-29709.  
7765007 D.B.Janssen, and J.P.Schanstra (1994).
Engineering proteins for environmental applications.
  Curr Opin Biotechnol, 5, 253-259.  
  7703850 E.V.Koonin, A.R.Mushegian, R.L.Tatusov, S.F.Altschul, S.H.Bryant, P.Bork, and A.Valencia (1994).
Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling.
  Protein Sci, 3, 2045-2054.  
8143720 H.Dirr, P.Reinemer, and R.Huber (1994).
X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
  Eur J Biochem, 220, 645-661.  
8108434 K.Berhane, M.Widersten, A.Engström, J.W.Kozarich, and B.Mannervik (1994).
Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases.
  Proc Natl Acad Sci U S A, 91, 1480-1484.  
  7538846 K.Lim, J.X.Ho, K.Keeling, G.L.Gilliland, X.Ji, F.Rüker, and D.C.Carter (1994).
Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV.
  Protein Sci, 3, 2233-2244.
PDB code: 1gne
7892174 K.Zeng, J.P.Rose, H.C.Chen, C.L.Strickland, C.P.Tu, and B.C.Wang (1994).
A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.
  Proteins, 20, 259-263.
PDB code: 1ags
7925413 P.Zimniak, B.Nanduri, S.Pikuła, J.Bandorowicz-Pikuła, S.S.Singhal, S.K.Srivastava, S.Awasthi, and Y.C.Awasthi (1994).
Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties.
  Eur J Biochem, 224, 893-899.  
  8206823 R.Bader, and T.Leisinger (1994).
Isolation and characterization of the Methylophilus sp. strain DM11 gene encoding dichloromethane dehalogenase/glutathione S-transferase.
  J Bacteriol, 176, 3466-3473.  
8290582 R.Zettl, J.Schell, and K.Palme (1994).
Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase.
  Proc Natl Acad Sci U S A, 91, 689-693.  
7765835 T.Leisinger, R.Bader, R.Hermann, M.Schmid-Appert, and S.Vuilleumier (1994).
Microbes, enzymes and genes involved in dichloromethane utilization.
  Biodegradation, 5, 237-248.  
8354272 A.Karshikoff, P.Reinemer, R.Huber, and R.Ladenstein (1993).
Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in pi-class glutathione transferases.
  Eur J Biochem, 215, 663-670.  
  8284939 D.J.Meyer (1993).
Significance of an unusually low Km for glutathione in glutathione transferases of the alpha, mu and pi classes.
  Xenobiotica, 23, 823-834.  
  8298459 F.A.Blocki, L.B.Ellis, and L.P.Wackett (1993).
MIF protein are theta-class glutathione S-transferase homologs.
  Protein Sci, 2, 2095-2102.  
8281936 F.Martini, A.Aceto, P.Sacchetta, T.Bucciarelli, B.Dragani, and C.Di Ilio (1993).
Investigation of intra-domain and inter-domain interactions of glutathione transferase P1-1 by limited chymotryptic cleavage.
  Eur J Biochem, 218, 845-851.  
8269591 J.E.Flatgaard, K.E.Bauer, and L.M.Kauvar (1993).
Isozyme specificity of novel glutathione-S-transferase inhibitors.
  Cancer Chemother Pharmacol, 33, 63-70.  
  8284946 J.H.Ploemen, B.van Ommen, J.J.Bogaards, and P.J.van Bladeren (1993).
Ethacrynic acid and its glutathione conjugate as inhibitors of glutathione S-transferases.
  Xenobiotica, 23, 913-923.  
8354281 P.Sacchetta, A.Aceto, T.Bucciarelli, B.Dragani, S.Santarone, N.Allocati, and C.Di Ilio (1993).
Multiphasic denaturation of glutathione transferase B1-1 by guanidinium chloride. Role of the dimeric structure on the flexibility of the active site.
  Eur J Biochem, 215, 741-745.  
9087540 R.A.Reiss, and A.A.James (1993).
A glutathione S-transferase gene of the vector mosquito, Anopheles gambiae.
  Insect Mol Biol, 2, 25-32.  
  8298458 R.W.Wang, A.W.Bird, D.J.Newton, A.Y.Lu, and W.M.Atkins (1993).
Fluorescence characterization of Trp 21 in rat glutathione S-transferase 1-1: microconformational changes induced by S-hexyl glutathione.
  Protein Sci, 2, 2085-2094.  
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.

 

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