Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine

Journal of Molecular Biology

Volumn 281, Issue 2, 1998, Pages 323-339

  Xiao, Gaoyi ^a   Parsons, James F ^b   Tesh, Kris ^b   Armstrong, Richard N ^b   Gilliland, Gary L ^a  

^a Ctr of Advanced Res in Biotechnol   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

3 fluorotyrosine; Detoxification enzyme; Glutathione transferase; Protein crystallography; Three dimensional structure

Indexed keywords

FLUORINE; GLUTATHIONE TRANSFERASE; TYROSINE; TYROSINE DERIVATIVE; WATER;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; RAT;

EID: 0032516767     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1935     Document Type: Article

References (39)

1. Armstrong R.N. Glutathione S-transferases structure and mechanism of an archetypical detoxication enzyme. Advances in Enzymology and Related Areas Molecular Biology. vol. 9:1994;1-44 John Wiley & Sons Inc
2. Armstrong R.N. Structure, catalytic mechanism and evolution of the glutathione transferases. Chem. Res. Toxicol. 10:1997;2-28
3. a of Tyr-6 in rat α1-1 GSH transferase. J. Biol. Chem. 268:1993;19188-19191
4. Bacon D.J., Anderson W.F. A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics. 6:1988;219-220
5. Bernstein F.C., Koetzle T.F., Williams G.J.B., Meyer E.F. Jr, Brice M.D., Rodgers 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;535-542
6. Brooks B., Benisek W.F. Mechanism of the reaction catalyzed by 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni kinetic properties of a modified enzyme in which tyrosine 14 is replaced by 3-fluorotyrosine. Biochemistry. 33:1994;2682-2687
7. Brünger A.T. X-PLOR Version 3.1: A System for X-ray Crystallography and NMR. 1992;Yale University Press, New Haven
8. Brünger A.T. Free R value a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475
9. 19F-NMR spectroscopy. Eur. J. Biochem. 278:1993;1041-1047
10. 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase equilibrium folding and ligand binding studies. Biochemistry. 33:1994;5502-5509
11. 19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy. Biochemistry. 35:1996;16843-16951
12. 19F nuclear magnetic resonance relaxation times and molecular motion of the individual fluorotyrosines. Biochemistry. 13:1974;3431-3437
13. Hull W.E., Sykes B.D. Fluorine-19 nuclear magnetic response studies of fluorotyrosine alkaline phosphatase the influence of Zinc on protein structure and a conformational change induced by phosphate binding. Biochemistry. 15:1976;1535-1543
14. James M.N., Sielecki A.R. Structure and refinement of penicillopepsin at 1.8 Å resolution. J. Mol. Biol. 163:1983;299-361
15. Jeffery G.A., Saenger W. Hydrogen Bonding in Biological Structures. 1991;Springer-Verlag
16. 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
17. Ji X., Zhang P., Johnson W.W., Sesay M.A., Dickert L., Prasad S.S., 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 crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry. 33:1994;1043-1052
18. Ji X., Zhang P., von Rosenvinge E.C., Johson W.W., Tomarev S.I., Piatigorsky J., Armstrong R.N., Gilliland G.L. The three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione S-transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry. 34:1995;5317-5328
19. Johnson W.W., Liu S., Ji X., Johnson W.W., 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
20. Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119
21. Jones T.A., Kjeldgaard M. O version 5.9.1. 1993;Department of Molecular Biology, BMC. Uppsala University, Sweden. and Department of Chemistry, Aarhus University, Denmark
22. Karshikoff A., Reinemer P., Huber R., Ladenstein R. Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in π-class glutathione transferases. Eur. J. Biochem. 215:1993;663-670
23. Kimber B.J., Griffiths D.V., Birdsall B., King R.W., Scudder P., Freeney J., Roberts G.C.K., Burgen A.S.V. Fluorine-19 nuclear magnetic response studies of ligand binding to 3-flurotyrosine- and 6-fluorotryptophan-containing dihydrofolate reductase from Lactobacillus casei. Biochemistry. 16:1977;3492-3500
24. 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
25. Liu S., Ji X., Gilliland G.L., Stevens W.J., Armstrong R.N. Second-sphere electrostatic effects in the active site of glutathione transferase. observation of an on-face hydrogen bond between the side-chain of threonine 13 and π-cloud of tyrosine 6 and its influence on catalysis. J. Am. Chem. Soc. 115:1993;7910-7911
26. Lui S.M., Cowan J.A. Studies of the electonic and dynamic properties of high-potential iron proteins by substitution with non-natural amino acids. 3-fluorotyrosine-modified Chromatium vinosum high-potential iron protein. J. Am. Chem. Soc. 116:1994;4483-4484
27. Merrit E.A., Murphy M.E.P. Raster3D version 2.0 a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873
28. Meyer D.J., Xia C., Coles B., Chen H., Reinemer P., Huber R., Ketterer B. Unusual reactivity of Tyr-7 of GSH transferase P1-1. Biochem. J. 293:1993;351-356
29. Navaza J. AMoRe Automated package for molecular replacement. Acta Crystallog. sect. 50:1994;157-163
30. Orozco M., Vega C., Parraga A., Garcia-Saez I., Coll M., Walsh S., Mantle T.M., Luque F.J. On the reaction mechanism of class Pi glutathione S-transferase. Proteins: Struct. Funct. Genet. 28:1997;530-542
31. Parsons J.F., Armstrong R.N. Proton configuration in the ground state and transition state of a glutathione transferase-catalyzed reaction inferred from the properties of tetradeca(3-fluorotyrosyl) glutathione transferase. J. Am. Chem. Soc. 118:1996;2295-2296
32. Reinemer P., Dirr H.W., Ladenstein R., Schafer 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
33. Roussel A., Inisan A.-G., Cambillau C. TURBO-FRODO, AFMB and Bio Graphics. 1996;Marseille, France
34. 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
35. 19F-NMR studies of ligand binding to 5-fluorotrptophan- and 3-fluorotyrosine-containing cyclic AMP receptor protein from Esherichia coli. Biochem. J. 266:1990;545-552
36. Thorson J.S., Chapman E., Murphy E.C., Schultz P.G. Linear free energy analysis of hydrogen bonding in proteins. J. Am. Chem. Soc. 117:1995;1157-1158
37. Tronrud D.E. The TNT Refinement Package. 1994;Oregon State Board of Higher Education
38. Xiao G., Liu X., Ji X., Zhang P., Johnson W.W., Chen J., 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
39. Xiao G., Parsons J.F., Armstrong R.N., Gilliland G.L. Crystal structure of tetradeca-(3-fluorotyrosyl)-glutathione transferase. J. Am. Chem. Soc. 119:1997;9325-9326