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PDBsum entry 1guh

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1guh
Jmol
Contents
Protein chain
221 a.a. *
Ligands
GSB ×4
* Residue conservation analysis
PDB id:
1guh
Name: Transferase
Title: Structure determination and refinement of human alpha class glutathione transferase a1-1, and a comparison with the mu and pi class enzymes
Structure: Glutathione s-transferase a1-1. Chain: a, b, c, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Biol. unit: Dimer (from PQS)
Resolution:
2.60Å     R-factor:   0.229    
Authors: I.Sinning,G.J.Kleywegt,T.A.Jones
Key ref: I.Sinning et al. (1993). Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J Mol Biol, 232, 192-212. PubMed id: 8331657
Date:
24-Feb-93     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08263  (GSTA1_HUMAN) -  Glutathione S-transferase A1
Seq:
Struc:
222 a.a.
221 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 = HX + R-S-glutathione
RX
+
glutathione
Bound ligand (Het Group name = GSB)
matches with 74.00% similarity
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     metabolic process   6 terms 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
J Mol Biol 232:192-212 (1993)
PubMed id: 8331657  
 
 
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
I.Sinning, G.J.Kleywegt, S.W.Cowan, P.Reinemer, H.W.Dirr, R.Huber, G.L.Gilliland, R.N.Armstrong, X.Ji, P.G.Board.
 
  ABSTRACT  
 
The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these domains via a network of hydrogen bonds and salt-links. In particular, the sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is completely buried in a hydrophobic pocket. The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain". The main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21384452 A.F.Thévenin, C.L.Zony, B.J.Bahnson, and R.F.Colman (2011).
GSTpi modulates JNK activity through a direct interaction with JNK substrate, ATF2.
  Protein Sci, 20, 834-848.  
  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.  
21283550 C.Tuzmen, and B.Erman (2011).
Identification of ligand binding sites of proteins using the gaussian network model.
  PLoS One, 6, e16474.  
  21495793 L.G.Higgins, and J.D.Hayes (2011).
Mechanisms of induction of cytosolic and microsomal glutathione transferase (GST) genes by xenobiotics and pro-inflammatory agents.
  Drug Metab Rev, 43, 92.  
  21401344 L.M.Balogh, and W.M.Atkins (2011).
Interactions of glutathione transferases with 4-hydroxynonenal.
  Drug Metab Rev, 43, 165-178.  
20085333 L.M.Balogh, I.Le Trong, K.A.Kripps, L.M.Shireman, R.E.Stenkamp, W.Zhang, B.Mannervik, and W.M.Atkins (2010).
Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal.
  Biochemistry, 49, 1541-1548.
PDB codes: 3ik7 3ik9
19634988 M.A.Wouters, S.W.Fan, and N.L.Haworth (2010).
Disulfides as redox switches: from molecular mechanisms to functional significance.
  Antioxid Redox Signal, 12, 53-91.  
19664689 S.P.Singh, L.Zimniak, and P.Zimniak (2010).
The human hGSTA5 gene encodes an enzymatically active protein.
  Biochim Biophys Acta, 1800, 16-22.  
18987134 B.D.Persson, S.Müller, D.M.Reiter, B.B.Schmitt, M.Marttila, C.V.Sumowski, S.Schweizer, U.Scheu, C.Ochsenfeld, N.Arnberg, and T.Stehle (2009).
An arginine switch in the species B adenovirus knob determines high-affinity engagement of cellular receptor CD46.
  J Virol, 83, 673-686.
PDB codes: 3exv 3exw 3f0y
19842715 H.J.Atkinson, and P.C.Babbitt (2009).
Glutathione transferases are structural and functional outliers in the thioredoxin fold.
  Biochemistry, 48, 11108-11116.  
19538182 I.Axarli, P.Dhavala, A.C.Papageorgiou, and N.E.Labrou (2009).
Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases.
  Biochem J, 422, 247-256.
PDB code: 3fhs
19618965 L.M.Balogh, I.Le Trong, K.A.Kripps, K.Tars, R.E.Stenkamp, B.Mannervik, and W.M.Atkins (2009).
Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals.
  Biochemistry, 48, 7698-7704.
PDB codes: 3i69 3i6a
18792041 D.F.Dourado, P.A.Fernandes, B.Mannervik, and M.J.Ramos (2008).
Glutathione transferase: new model for glutathione activation.
  Chemistry, 14, 9591-9598.  
18342614 E.Connell, P.Scott, and B.Davletov (2008).
Real-time assay for monitoring membrane association of lipid-binding domains.
  Anal Biochem, 377, 83-88.  
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.  
18703268 N.Kinsley, Y.Sayed, S.Mosebi, R.N.Armstrong, and H.W.Dirr (2008).
Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1.
  Biophys Chem, 137, 100-104.  
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.  
16421451 E.Grahn, M.Novotny, E.Jakobsson, A.Gustafsson, L.Grehn, B.Olin, D.Madsen, M.Wahlberg, B.Mannervik, and G.J.Kleywegt (2006).
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.
  Acta Crystallogr D Biol Crystallogr, 62, 197-207.
PDB codes: 1pkw 1pkz 1pl1 1pl2 1xwg
16672236 J.L.Hearne, and R.F.Colman (2006).
Contribution of the mu loop to the structure and function of rat glutathione transferase M1-1.
  Protein Sci, 15, 1277-1289.  
16358001 S.Hederos, L.Tegler, J.Carlsson, B.Persson, J.Viljanen, and K.S.Broo (2006).
A promiscuous glutathione transferase transformed into a selective thiolester hydrolase.
  Org Biomol Chem, 4, 90-97.  
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.  
16189827 D.J.Schuller, Q.Liu, I.A.Kriksunov, A.M.Campbell, J.Barrett, P.M.Brophy, and Q.Hao (2005).
Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.
  Proteins, 61, 1024-1031.
PDB code: 1tw9
16154081 F.Angelucci, P.Baiocco, M.Brunori, L.Gourlay, V.Morea, and A.Bellelli (2005).
Insights into the catalytic mechanism of glutathione S-transferase: the lesson from Schistosoma haematobium.
  Structure, 13, 1241-1246.  
15757902 H.W.Dirr, T.Little, D.C.Kuhnert, and Y.Sayed (2005).
A conserved N-capping motif contributes significantly to the stabilization and dynamics of the C-terminal region of class Alpha glutathione S-transferases.
  J Biol Chem, 280, 19480-19487.  
15590633 P.Koivunen, K.E.Salo, J.Myllyharju, and L.W.Ruddock (2005).
Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.
  J Biol Chem, 280, 5227-5235.  
16108014 S.Hederos, and L.Baltzer (2005).
Nucleophile selectivity in the acyl transfer reaction of a designed enzyme.
  Biopolymers, 79, 292-299.  
15347687 L.A.Ralat, and R.F.Colman (2004).
Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site.
  J Biol Chem, 279, 50204-50213.  
15152091 M.A.Vargo, and R.F.Colman (2004).
Heterodimers of wild-type and subunit interface mutant enzymes of glutathione S-transferase A1-1: interactive or independent active sites?
  Protein Sci, 13, 1586-1593.  
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
15454730 N.Tetlow, M.Coggan, M.G.Casarotto, and P.G.Board (2004).
Functional polymorphism of human glutathione transferase A3: effects on xenobiotic metabolism and steroid biosynthesis.
  Pharmacogenetics, 14, 657-663.  
15077012 N.Tetlow, and P.G.Board (2004).
Functional polymorphism of human glutathione transferase A2.
  Pharmacogenetics, 14, 111-116.  
15333749 S.Hederos, K.S.Broo, E.Jakobsson, G.J.Kleywegt, B.Mannervik, and L.Baltzer (2004).
Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1.
  Proc Natl Acad Sci U S A, 101, 13163-13167.
PDB code: 1usb
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.  
12414796 G.K.Kong, G.Polekhina, W.J.McKinstry, M.W.Parker, B.Dragani, A.Aceto, D.Paludi, D.R.Principe, B.Mannervik, and G.Stenberg (2003).
Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1.
  J Biol Chem, 278, 1291-1302.
PDB codes: 1md3 1md4
14623980 K.Fritz-Wolf, A.Becker, S.Rahlfs, P.Harwaldt, R.H.Schirmer, W.Kabsch, and K.Becker (2003).
X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.
  Proc Natl Acad Sci U S A, 100, 13821-13826.
PDB code: 1okt
14573868 L.A.Ralat, and R.F.Colman (2003).
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.
  Protein Sci, 12, 2575-2587.  
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
12624100 R.E.Laliberte, D.G.Perregaux, L.R.Hoth, P.J.Rosner, C.K.Jordan, K.M.Peese, J.F.Eggler, M.A.Dombroski, K.F.Geoghegan, and C.A.Gabel (2003).
Glutathione s-transferase omega 1-1 is a target of cytokine release inhibitory drugs and may be responsible for their effect on interleukin-1beta posttranslational processing.
  J Biol Chem, 278, 16567-16578.  
12596270 R.M.Cardoso, D.S.Daniels, C.M.Bruns, and J.A.Tainer (2003).
Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum.
  Proteins, 51, 137-146.
PDB codes: 1m99 1m9a 1m9b
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.  
11872752 A.S.Johansson, and B.Mannervik (2002).
Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3.
  J Biol Chem, 277, 16648-16654.  
12211029 I.Le Trong, R.E.Stenkamp, C.Ibarra, W.M.Atkins, and E.T.Adman (2002).
1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site.
  Proteins, 48, 618-627.
PDB codes: 1k3l 1k3o 1k3y
12192076 J.K.Luo, J.A.Hornby, L.A.Wallace, J.Chen, R.N.Armstrong, and H.W.Dirr (2002).
Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases.
  Protein Sci, 11, 2208-2217.  
12108547 P.Harwaldt, S.Rahlfs, and K.Becker (2002).
Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target.
  Biol Chem, 383, 821-830.  
12023294 P.L.Pettersson, A.S.Johansson, and B.Mannervik (2002).
Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase.
  J Biol Chem, 277, 30019-30022.  
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
11297419 B.S.Nieslanik, C.Ibarra, and W.M.Atkins (2001).
The C-terminus of glutathione S-transferase A1-1 is required for entropically-driven ligand binding.
  Biochemistry, 40, 3536-3543.  
11524005 C.Ibarra, B.S.Nieslanik, and W.M.Atkins (2001).
Contribution of aromatic-aromatic interactions to the anomalous pK(a) of tyrosine-9 and the C-terminal dynamics of glutathione S-transferase A1-1.
  Biochemistry, 40, 10614-10624.  
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
10744731 G.Stenberg, B.Dragani, R.Cocco, B.Mannervik, and A.Aceto (2000).
A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1.
  J Biol Chem, 275, 10421-10428.  
11101503 I.Schmidt-Krey, K.Mitsuoka, T.Hirai, K.Murata, Y.Cheng, Y.Fujiyoshi, R.Morgenstern, and H.Hebert (2000).
The three-dimensional map of microsomal glutathione transferase 1 at 6 A resolution.
  EMBO J, 19, 6311-6316.  
10737945 J.U.Flanagan, W.King, M.W.Parker, P.G.Board, and G.Chelvanayagam (2000).
Ab initio calculations on hidden modulators of theta class glutathione transferase activity.
  Proteins, 39, 235-243.  
10681528 J.Wang, S.Bauman, and R.F.Colman (2000).
Probing subunit interactions in alpha class rat liver glutathione S-transferase with the photoaffinity label glutathionyl S-[4-(succinimidyl)benzophenone].
  J Biol Chem, 275, 5493-5503.  
10900265 L.O.Nilsson, A.Gustafsson, and B.Mannervik (2000).
Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.
  Proc Natl Acad Sci U S A, 97, 9408-9412.  
10883816 M.Ishigai, J.I.Langridge, R.S.Bordoli, and S.J.Gaskell (2000).
Noncovalent associations of glutathione S-transferase and ligands: a study using electrospray quadrupole/time-of-flight mass spectrometry.
  J Am Soc Mass Spectrom, 11, 606-614.  
10984526 P.C.Babbitt (2000).
Reengineering the glutathione S-transferase scaffold: a rational design strategy pays off.
  Proc Natl Acad Sci U S A, 97, 10298-10300.  
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.  
11027134 Y.Gu, S.V.Singh, and X.Ji (2000).
Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide.
  Biochemistry, 39, 12552-12557.
PDB codes: 1f3a 1f3b
10652317 Y.V.Patskovsky, L.N.Patskovska, and I.Listowsky (2000).
The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases.
  J Biol Chem, 275, 3296-3304.
PDB code: 2gtu
10587450 A.Gustafsson, M.Etahadieh, P.Jemth, and B.Mannervik (1999).
The C-terminal region of human glutathione transferase A1-1 affects the rate of glutathione binding and the ionization of the active-site Tyr9.
  Biochemistry, 38, 16268-16275.  
10346919 B.S.Nieslanik, M.J.Dabrowski, R.P.Lyon, and W.M.Atkins (1999).
Stopped-flow kinetic analysis of the ligand-induced coil-helix transition in glutathione S-transferase A1-1: evidence for a persistent denatured state.
  Biochemistry, 38, 6971-6980.  
9929473 C.C.Chuang, S.H.Wu, S.H.Chiou, and G.G.Chang (1999).
Homology modeling of cephalopod lens S-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity.
  Biophys J, 76, 679-690.  
10569948 H.W.Dirr, and L.A.Wallace (1999).
Role of the C-terminal helix 9 in the stability and ligandin function of class alpha glutathione transferase A1-1.
  Biochemistry, 38, 15631-15640.  
  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.  
10600132 L.A.Wallace, and H.W.Dirr (1999).
Folding and assembly of dimeric human glutathione transferase A1-1.
  Biochemistry, 38, 16686-16694.  
10451545 L.Stella, M.Nicotra, G.Ricci, N.Rosato, and E.E.Di Iorio (1999).
Molecular dynamics simulations of human glutathione transferase P1-1: analysis of the induced-fit mechanism by GSH binding.
  Proteins, 37, 1-9.  
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.  
9930979 Y.V.Patskovsky, L.N.Patskovska, and I.Listowsky (1999).
Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a.
  Biochemistry, 38, 1193-1202.
PDB code: 1gtu
9839448 A.Pastore, M.Lo Bello, G.Aureli, G.Federici, G.Ricci, C.Di Ilio, and R.Petruzzelli (1998).
Purification and characterization of a novel alpha-class glutathione transferase from human liver.
  Int J Biochem Cell Biol, 30, 1235-1243.  
  9495016 B.Favaloro, S.Melino, R.Petruzzelli, C.Di Ilio, and D.Rotilio (1998).
Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi.
  FEMS Microbiol Lett, 160, 81-86.  
9792709 J.H.Choi, W.Lou, and A.Vancura (1998).
A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae.
  J Biol Chem, 273, 29915-29922.  
9799517 J.M.Stevens, J.A.Hornby, R.N.Armstrong, and H.W.Dirr (1998).
Class sigma glutathione transferase unfolds via a dimeric and a monomeric intermediate: impact of subunit interface on conformational stability in the superfamily.
  Biochemistry, 37, 15534-15541.  
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.  
9843371 J.Wang, S.Bauman, and R.F.Colman (1998).
Photoaffinity labeling of rat liver glutathione S-transferase, 4-4, by glutathionyl S-[4-(succinimidyl)-benzophenone].
  Biochemistry, 37, 15671-15679.  
9548764 L.A.Wallace, N.Sluis-Cremer, and H.W.Dirr (1998).
Equilibrium and kinetic unfolding properties of dimeric human glutathione transferase A1-1.
  Biochemistry, 37, 5320-5328.  
9761928 L.N.Patskovska, A.A.Fedorov, Y.V.Patskovsky, S.C.Almo, and I.Listowsky (1998).
Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2.
  Acta Crystallogr D Biol Crystallogr, 54, 458-460.  
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.  
9818187 S.D.Copley (1998).
Microbial dehalogenases: enzymes recruited to convert xenobiotic substrates.
  Curr Opin Chem Biol, 2, 613-617.  
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.  
9218781 A.D.Cameron, B.Olin, M.Ridderström, B.Mannervik, and T.A.Jones (1997).
Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping.
  EMBO J, 16, 3386-3395.
PDB code: 1fro
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
9188739 A.Marsh, and D.M.Ferguson (1997).
Knowledge-based modeling of a bacterial dichloromethane dehalogenase.
  Proteins, 28, 217-226.  
9325266 B.Dragani, G.Stenberg, S.Melino, R.Petruzzelli, B.Mannervik, and A.Aceto (1997).
The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability.
  J Biol Chem, 272, 25518-25523.  
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.  
  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.  
9287168 L.O.Hansson, M.Widersten, and B.Mannervik (1997).
Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions.
  Biochemistry, 36, 11252-11260.  
9407009 M.J.Snyder, and D.R.Maddison (1997).
Molecular phylogeny of glutathione-S-transferases.
  DNA Cell Biol, 16, 1373-1384.  
  9260294 M.Kuge, Y.Fujii, T.Shimizu, F.Hirose, A.Matsukage, and T.Hakoshima (1997).
Use of a fusion protein to obtain crystals suitable for X-ray analysis: crystallization of a GST-fused protein containing the DNA-binding domain of DNA replication-related element-binding factor, DREF.
  Protein Sci, 6, 1783-1786.  
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.  
  9045797 S.Vuilleumier (1997).
Bacterial glutathione S-transferases: what are they good for?
  J Bacteriol, 179, 1431-1441.  
  9098897 W.M.Atkins, E.C.Dietze, and C.Ibarra (1997).
Pressure-dependent ionization of Tyr 9 in glutathione S-transferase A1-1: contribution of the C-terminal helix to a "soft" active site.
  Protein Sci, 6, 873-881.  
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
8663359 D.V.Lueder, and M.A.Phillips (1996).
Characterization of Trypanosoma brucei gamma-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione (diglutathionylspermidine).
  J Biol Chem, 271, 17485-17490.  
8810897 E.C.Dietze, C.Ibarra, M.J.Dabrowski, A.Bird, and W.M.Atkins (1996).
Rational modulation of the catalytic activity of A1-1 glutathione S-transferase: evidence for incorporation of an on-face (pi...HO-Ar) hydrogen bond at tyrosine-9.
  Biochemistry, 35, 11938-11944.  
8639625 E.C.Dietze, R.W.Wang, A.Y.Lu, and W.M.Atkins (1996).
Ligand effects on the fluorescence properties of tyrosine-9 in alpha 1-1 glutathione S-transferase.
  Biochemistry, 35, 6745-6753.  
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
8736558 J.Qin, G.M.Clore, W.P.Kennedy, J.Kuszewski, and A.M.Gronenborn (1996).
The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.
  Structure, 4, 613-620.
PDB codes: 1cqg 1cqh
  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.  
8790344 N.Mouz, C.Tricot, C.Ebel, Y.Petillot, V.Stalon, and O.Dideberg (1996).
Use of a designed fusion protein dissociates allosteric properties from the dodecameric state of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase.
  Proc Natl Acad Sci U S A, 93, 9414-9419.  
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.  
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.  
8654388 S.I.Tomarev, and J.Piatigorsky (1996).
Lens crystallins of invertebrates--diversity and recruitment from detoxification enzymes and novel proteins.
  Eur J Biochem, 235, 449-465.  
8937881 S.S.Tang, C.C.Lin, and G.G.Chang (1996).
Metal-catalyzed oxidation and cleavage of octopus glutathione transferase by the Cu(II)-ascorbate system.
  Free Radic Biol Med, 21, 955-964.  
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.  
  8770536 J.D.Hayes, and D.J.Pulford (1995).
The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.
  Crit Rev Biochem Mol Biol, 30, 445-600.  
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.  
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.  
7675787 M.A.McTigue, S.L.Bernstein, D.R.Williams, and J.A.Tainer (1995).
Purification and crystallization of a schistosomal glutathione S-transferase.
  Proteins, 22, 55-57.  
  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.  
8590004 M.Saarinen, F.K.Gleason, and H.Eklund (1995).
Crystal structure of thioredoxin-2 from Anabaena.
  Structure, 3, 1097-1108.
PDB code: 1thx
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.  
  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.  
  7888077 F.Morel, W.A.Schulz, and H.Sies (1994).
Gene structure and regulation of expression of human glutathione S-transferases alpha.
  Biol Chem Hoppe Seyler, 375, 641-649.  
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.  
7702742 S.S.Tang, C.C.Lin, and G.G.Chang (1994).
Isolation and characterization of octopus hepatopancreatic glutathione S-transferase. Comparison of digestive gland enzyme with lens S-crystallin.
  J Protein Chem, 13, 609-618.  
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.  
  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.  
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