Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles of Cys10 and His106

Journal of Molecular Biology

Volumn 281, Issue 1, 1998, Pages 135-147

  Nishida, Motohiko ^a   Harada, Shigeharu ^a   Noguchi, Shuji ^a   Satow, Yoshinori ^a   Inoue, Hideshi ^b   Takahashi, Kenji ^b  

^a TOKYO UNIVERSITY OF SCIENCE   (Japan)

^b TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

Crystal structure; Detoxification; Escherichia coli; Glutathione; Glutathione S transferase

Indexed keywords

BACTERIAL ENZYME; DIMER; ENZYME INHIBITOR; GLUTATHIONE DERIVATIVE; GLUTATHIONE TRANSFERASE; SULFONIC ACID DERIVATIVE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME INHIBITOR COMPLEX; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA;

EID: 0032493846     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1927     Document Type: Article

References (48)

1. Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10:1997;2-18
2. Bernstein F.C., Koetzle T.F., Williams G.J.B., Meyer E.F. Jr, Brice M.D., Rogers J.R., Kennard O., Shimanouchi T., Tasumi M. The Protein Data Bank a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:1977;535-547
3. Björnestedt R., Stenberg G., Widersten M., Board P.G., Sinning I., Jones T.A., Mannervik B. Functional significance of arginine 15 in the active site of human class alpha glutathione transferase A1-1. J. Mol. Biol. 247:1995;765-773
4. Board P.G., Coggan M., Wilce M.C.J., Parker M.W. Evidence for an essential serine residue in the active site of the theta class glutathione transferases. Biochem. J. 311:1995;247-250
5. Brünger A.T. X-PLOR Version 3. 1: A System for X-ray Crystallography and NMR. 1992;Yale University, New Haven, CT, USA
6. Coles B., Ketterer B. The role of glutathione and glutathione transferases in chemical carcinogenesis. CRC Crit. Rev. Biochem. Mol. Biol. 25:1990;47-70
7. Acta Crystallog. sect. D. 50:1994;760-763
8. Cowtan K.D., Main P. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallog. sect. D. 52:1996;43-48
9. Daniel V. Glutathione S-transferases gene structure and regulation of expression. CRC Crit. Rev. Biochem. Mol. Biol. 28:1993;173-207
10. Di Ilio C., Aceto A., Allocati N., Piccolomini R., Bucciarelli T., Dragani B., Faraone A., Sacchetta P., Petruzzelli R., Federici G. Characterization of glutathione transferase from Xanthomonas campestris. Arch. Biochem. Biophys. 305:1993;110-114
11. Dirr H., Reinemer P., Huber R. Refined crystal structure of porcine class pi glutathione S-transferase (pGST P1-1) at 2.1 Å resolution. J. Mol. Biol. 243:1994;72-92
12. Dirr H., Reinemer P., Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220:1994;645-661
13. Hofer B., Backhaus S., Timmis K.N. The biphenyl/polychlorinated biphenyl-degradation locus (bph) of Pseudomonas sp. LB400 encodes four additional metabolic enzymes. Gene. 144:1994;9-16
14. Inoue H., Nishida M., Satow Y., Takahashi K. Study using site-directed mutagenesis on glutathione transferase from Eschericha coli. The Proceedings of International Workshop on Glutathione Transferases. 1997;72 University of Rome Tor Vergata, Rome, Italy
15. Ishigaki S., Abramovitz M., Listowsky I. Glutathione-S-transferases are major cytosolic thyroid hormone binding proteins. Arch. Biochem. Biophys. 273:1989;265-272
16. Jensson H., Guthenberg C., Ålin P., Mannervik B. Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals. FEBS Letters. 208:1986;207-209
17. Ji X., Zhang P., Armstrong R.N., Gilliland G.L. The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-Å resolution. Biochemistry. 31:1992;10169-10184
18. Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J., Armstrong R.N., Gilliland G.L. Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry. 34:1995;5317-5328
19. Ji X., von Rosenvinge E.C., Johnson W.W., Armstrong R.N., Gilliland G.L. Location of a potential transport binding site in a sigma class glutathione transferase by X-ray crystallography. Proc. Natl Acad. Sci. USA. 93:1996;8208-8213
20. Kabsch W., Sander C. Dictionary of protein secondary structure pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637
21. Kong K.-H., Inoue H., Takahashi K. Site-directed mutagenesis of amino acid residues involved in the glutathione binding of human glutathione S-transferase P1-1. J. Biochem. 112:1992;725-728
22. Kraulis P.J. MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
23. La Roche S.D., Leisinger T. Sequence analysis and expression of the bacterial dichloromethane dehalogenase structural gene, a member of the glutathione S-transferase supergene family. J. Bacteriol. 172:1990;164-171
24. Listowsky I., Abramovitz M., Homma H., Niitsu Y. Intracellar binding and transport of hormones and xenobiotics by glutathione S-transferases. Drug Metabol. Rev. 19:1988;305-318
25. Luzzati P.V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810
26. Mannervik B., Danielson U.H. Glutathione transferases - structure and catalytic activity. CRC Crit. Rev. Biochem. Mol. Biol. 23:1988;283-337
27. Mannervik B., Awasthi Y.C., Board P.G., Hayes J.D., Ilio C.D., Ketterer B., Liskowsky I., Morgenstern R., Muramatsu M., Pearson W.R., Pickett C.B., Sato K., Widersten M., Wolf C.R. Nomenclature for human glutathione transferases. Biochem. J. 282:1992;305-308
28. Masai E., Katayama Y., Kubota S., Kawai S., Yamasaki M., Morohoshi N. A bacteiral enzyme degrading the model lignin compound β-etherase is a member of the glutathione-S-transferase superfamily. FEBS Letters. 323:1993;135-140
29. McTigue M.A., Williams D.R., Tainer J.A. Crystal structures of a schistosomal drug and vactine target glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J. Mol. Biol. 246:1995;21-27
30. Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B. Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione evidence for an induced-fit mechanism. J. Mol. Biol. 274:1997;446-453
31. Nishida M., Kong K.-H., Inoue H., Takahashi K. Molecular cloning and site directed mutagenesis of glutathione S-transferase from Escherichia coli. The conserved tyrosine residue near the N-terminus in not essential for catalysis. J. Biol. Chem. 269:1994;32536-32541
32. Nishida M., Harada S., Satow Y., Inoue H., Takahashi K. Crystallization and X-ray diffraction studies of glutathione S-transferase from Escherichia coli. J. Crystal Growth. 168:1996;284-287
33. Orser C.S., Dutton J., Lange C., Jablonski P., Xun L., Hargis M. Characterization of a Flavobacterium glutathione S-transferase gene involved in reductive dechlorination. J. Bacteriol. 175:1993;2640-2644
34. Otwinowski Z. An Oscillation Data Processing Suite for Macromolecular Crystallography. 1992;Yale University, New Haven, CT, USA
35. Pemble S.E., Taylor J.B. An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences. Biochem. J. 287:1992;957-963
36. Perito B., Allocati N., Casalone E., Masulli M., Dragani B., Polsinelli M., Aceto A., Di Ilio C. Molecular cloning and overexpression of a glutathione transferase gene from Proteus mirabilis. Biochem. J. 318:1996;157-162
37. Ramakrishnan C., Ramachandran G.N. Stereochemical criteria for polypeptide and protein chain conformation. Biophys. J. 5:1965;909-933
38. Reinemer P., Dirr H.W., Ladenstein R., Schäffer J., Gallay O., Huber R. The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1991;1997-2005
39. Reinemer P., Dirr H.W., Ladenstein R., Huber R. Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227:1992;214-226
40. Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R., Palme K., Schell J., Koelln I., Bartunik H.D., Bieseler B. Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 Å resolution structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J. Mol. Biol. 255:1996;289-309
41. Roussel A., Cambillau C. Turbo-FRODO, Version 5.4. 1995;Faculté de Médecine Nord, Marseille, France
42. Rushmore T.H., Pickett C.B. Glutathione S-transferases, structure, regulation, and therapeutic implications. J. Biol. Chem. 268:1993;11475-11478
43. Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W., Huber R., Gilliland G.L., Armstrong R.N., Ji X., Board P.G., Olin B., Mannervik B., Jones T.A. 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. 232:1993;192-212
44. Vuilleumier S., Leisinger T. Protein engineering studies of dichloromethane dehalogenase/glutathione S-transferase from Methylophilus sp. strain DM11. Ser12 but not Tyr6 is required for enzyme activity. Eur. J. Biochem. 239:1996;410-417
45. Wang R.W., Newton D.J., Johnson A.R., Pickett C.B., Lu A.Y.H. Site-directed mutagenesis of glutathione S-transferase YaYa. Mapping the glutathione-binding site. J. Biol. Chem. 268:1993;23981-23985
46. Widersten M., Kolm R.H., Björnestedt R., Mannervik B. Contribution of five amino acid residues in the glutathione-binding site to the function of human glutathione transferase P1-1. Biochem. J. 285:1992;377-381
47. Wilce M.C.J., Parker M.W. Structure and function of glutathione S-transferases. Biochim. Biopys. Acta. 1205:1994;1-18
48. Wilce M.C.J., Board P.G., Feil S.C., Parker M.W. Crystal structure of a theta-class glutathione transferase. EMBO J. 14:1995;2133-2143