The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94 Å resolution

Journal of Molecular Biology

Volumn 278, Issue 1, 1998, Pages 239-252

  Sun, Yuh Ju ^a   Kuan, I Ching ^a   Tam, Ming F ^a   Hsiao, Chwan Deng ^a  

^a INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

Author keywords

Epoxidase activity; Glutathione S transferase; S hexyl glutathione; X ray crystallography; Y115F mutant

Indexed keywords

(9S,10S) 9 (S GLUTATHIONYL) 10 HYDROXY 9,10 DIHYDROPHENANTHRENE; 1 CHLORO 2,4 DINITROBENZENE; EPOXIDASE; GLUTATHIONE TRANSFERASE; PHENANTHRENE DERIVATIVE; PHENYLALANINE; PROTEIN SUBUNIT; S HEXYLGLUTATHIONE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; FOWL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

EID: 0032562548     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1716     Document Type: Article

References (53)

1. b3 gene in rat brain. J. Biol. Chem. 262:1987;7770-7773
2. b3 glutathione S-transferase in Escherichia coli and identification of its natural form in rat brain. J. Biol. Chem. 263:1988;17627-17631
3. Ålin P., Jensson H., Guthenberg C., Danielson U.H., Tahir M.K., Mannervik B. Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing. Anal. Biochem. 146:1985;313-320
4. Armstrong R.N. GSTs reaction mechanism, structure and function. Chem. Res. Toxicol. 4:1991;131-140
5. Bernstein F.C., Koetzle T.F., Williams G.J.B., Meyer E.F.J., Brice M.D., Rodgers J.R., Kennard O., Shimanouchi T., Tsaumi M. The Protein Data Bank a computer-based archival file for macromolecular structure. J. Mol. Biol. 112:1977;535-542
6. Bhargava M.M., Listowsky I., Arias I.M. Ligandin. Bilirubin binding and GST activity are independent processes. J. Biol. Chem. 253:1978;4112-4115
7. Brunger A.T. Extension of molecular replacement a new search strategy based on Patterson correlation refinement. Acta Crystallog. sect. A. 46:1990;46-57
8. Brunger A.T. Free R value a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475
9. Brunger A.T., Krukowski A. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallog. sect. A. 46:1990;585-593
10. Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F. Characterization of glutathione S-transfeases from day-old chick livers. Biochemistry. 29:1990;744-750
11. Christ-Hazelhof E., Nutgeren D. Purification and characterization of prostaglandin endoperoxide D-isomerase, a cytoplasmic, glutathione-requiring enzyme. Biochim. Biophys. Acta. 572:1979;43-51
12. Craig S.P. III, Yuan L., Kuntz D.A., McKerrow J.H., Wang C.C. High level expression in Escherichia coli of soluble, enzymatically active schistosomal hypoxanthine/guanine phosphoribosyltransferase and trypanosomal ornithine de carboxylase. Proc. Natl Acad. Sci. USA. 88:1991;2500-2504
13. Danielson H., Esterbauer H., Mannervik B. Structure-activity relationships of 4-hydroxylalkenals in the conjugation catalyzed by mammalian glutathione transferases. Biochem. J. 247:1987;707-713
14. Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326
15. Gribskov M., Burgess R.R. Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins. Nucl. Acids Res. 14:1986;6745-6763
16. Habig W.H., Pabst M.J., Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:1974;7130-7139
17. Hayes J.D., Pulford D.J. The glutathione S-transferase supergene family regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. CRC Crit. Rev. Biochem. Mol. Biol. 30:1995;445-600
18. Hsieh C.-H., Tsai S.-P., Yeh H.-I., Sheu T.-C., Tam M.F. Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases. Identification of a novel class-alpha GST, rGSTA6*, in rat testis. Biochem. J. 323:1997;503-510
19. Hu L.Q., Colman R.F. Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3. J. Biol. Chem. 270:1995;21875-21883
20. Ishigaki S., Abramovitz M., Listowsky I. Glutathione-S-transferases are major cytosolic thyroid hormone binding proteins. Arch. Biochem. Biophys. 273:1989;265-272
21. 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
22. Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L., Armstrong R.N., Gilliland G.L. Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallograpic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry. 33:1994;1043-1052
23. Johnson J.A., Finn K.A., Siegel F.L. Tissue distribution of enzymic methylation of GST and its effects on catalytic activity. Methylation of GST 11-11 inhibits conjugating activity towards CDNB. Biochem. J. 282:1992;279-289
24. Johnson W.W., Liu S., Ji X., Gilliland G.L., Armstrong R.N. Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase. J. Biol. Chem. 268:1993;11508-11511
25. Kraulis P.J. Molscript a program to produce both detail and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
26. Kubo Y., Armstrong R.N. Observation of a substituent effect on the stereoselectivity of glutathione S-transferase toward para-substituted 4-phenyl-3-buten-2-ones. Chem. Res. Toxicol. 2:1989;144-145
27. Lai H.-C.J., Grove G., Tu C.-P.D. Cloning and sequence analysis of a cDNA for a rat liver GST Yb subunit. Nucl. Acids Res. 14:1986;6101-6114
28. Lawrence R.A., Burk R.F. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 71:1976;952-958
29. Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C. Three-dimensional strucutre of Schistosoma japonicum GST fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3:1994;2233-2244
30. Liu L.-F., Tam M.F. Nucleotide sequence of a class μ glutathione S-transferase from chicken liver. Biochim. Biophys. Acta. 1090:1991;343-344
31. Liu L.-F., Hong J.-L., Tsai S.-P., Hsieh J.-C., Tam M.F. Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2,4-dinitrobenzene specific labelling of Tyr-115. Biochem. J. 296:1993;189-197
32. Liu L.-F., Liaw Y.C., Tam M.F. Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their site-directed mutants heterologously expressed in Escherichia coli identification of Lys15 and Ser208 on cGSTA1-1 as residues interacting with ethacrynic acid. Biochem. J. 327:1997;593-600
33. Liu S., Zhang P., Ji X., Johnson W.W., Gilliland G.L., Armstrong R.N. Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase. J. Biol. Chem. 267:1992;4296-4299
34. Mannervik B., Danielson U.H. Glutathione transferases-structure and catalytic activity. CRC Crit. Rev. Biochem. 23:1988;283-337
35. Mannervik B., Ålin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Jornvall H. Identification of three classes of cytosolic glutathione transferases common to several mammalian species correlation between structural data and enzymatic properties. Proc. Natl Acad. Sci. USA. 82:1985;7202-7206
36. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497
37. Meyer D.J., Thomas M. Characterization of rat spleen prostaglandin H D -isomerase as a sigma class GSH transferase. Biochem. J. 311:1995;739-742
38. Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B. Theta, a new class of glutathione transferases purified from rat and man. Biochem. J. 274:1991;409-414
39. Otwinowski Z. Sawyer L., Isaacs N., Bailey S. Editor of Data Collection and Processing. Proceedings of the CCP4 Study Weekend. 1993;SERC, Daresbury Laboratory, Warrington, U.K
40. Pemble S.E., Wardle A.F., Taylor J.B. Glutathione S-transferase class kappa characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem. J. 319:1996;749-754
41. Penington C.J., Rule G.S. Mapping the substrate-binding site of a human class mu glutathione transferase using magnetic resonance spectroscopy. Biochemistry. 31:1992;2912-2920
42. Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J., Penington C.J., Rule G.S. Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J. Mol. Biol. 238:1994;815-832
43. Ramakrishnan C., Ramachandran G.N. Stereochemical criteria for polypeptide and protein chain conformation. Biophys. J. 5:1965;909-933
44. Reinemer P., Dirr H.W., Ladenstein R., Schaffer J., Gallay O., Huber R. The 3-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1991;1997-2005
45. Ricci G., Caccuri A.M., Lobello M., Rosato N., Mei G., Nicotra M., Chiessi E., Mazzetti A.O., Federici G. Structural flexibility modulates the activity of human glutathione transferase P1-1 - role of helix 2 flexibility in the catalytic mechanism. J. Biol. Chem. 271:1996;16187-16192
46. Shan S.-O., Armstrong R.N. Rational reconstruction of the active site of a class mu GST. J. Biol. Chem. 269:1994;32373-32379
47. Shen T.-J., Ho N.T., Simplaceanu V., Zou M., Green B.N., Tam M.F., Ho C. Production of unmodified human adult hemoglobin in Escherichia coli. Proc. Natl Acad. Sci. USA. 90:1993;8108-8112
48. 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
49. Tan K.H., Meyer D.J., Coles B., Ketterer B. Thymine hydroperoxide, a substrate for rat Se-dependent glutathione peroxidase and glutathione transferase isoenzymes. FEBS Letters. 207:1986;231-233
50. Vorachek W.R., Pearson W.R., Rule G.S. Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc. Natl Acad. Sci. USA. 88:1991;4443-4447
51. Widersten M., Bjornestedt R., Mannervik B. Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1. Biochemistry. 35:1996;7731-7742
52. Xiao G.Y., Liu S.X., Ji X.H., Johnson W.W., Chen J.H., Parsons J.F., Stevens W.J., Gilliland G.L., Armstrong R.N. First-sphere and second-sphere electrostatic effects in the active site of a class mu glutathione transferase. Biochemistry. 35:1996;4753-4765
53. Yeh H.-I., Hsieh C.-H., Wang L.-Y., Tsai S.-P., Hsu H.-Y., Tam M.F. Mass spectrometric analysis of rat liver cytoslic glutathione S-transferases modifications are limited to N-terminal processing. Biochem. J. 308:1995;69-75