A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: Crystal structure of Spo0F from Bacillus subtilis

Biochemistry

Volumn 36, Issue 42, 1997, Pages 12739-12745

  Madhusudan, ^a   Zapf, James ^a   Hoch, James A ^a   Whiteley, John M ^a   Xuong, Nguyen H ^b   Varughese, Kottayil I ^a,b  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CALCIUM ION; HISTIDINE; MUTANT PROTEIN; PHOSPHOTRANSFERASE; PROTEIN KINASE; REGULATOR PROTEIN;

ANTIBIOTIC SENSITIVITY; ARTICLE; BACILLUS SUBTILIS; BINDING SITE; CHEMOTAXIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SPOROGENESIS;

AMINO ACID SUBSTITUTION; ARGININE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CALCIUM; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SECOND MESSENGER SYSTEMS;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 0030660409     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971276v     Document Type: Article

References (44)

1. Alatossava, T., Jutte, H., Kuhn, A., & Kellenberger, E. (1985) J. Bacteriol. 162, 413-419.
2. Alex, L. A., Borkovich, K. A., & Simon, M. I. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 3416-3421.
3. Baikalov, I., Schroder, I., Kaczor-Grzeskowiak, M., Greskowiak, K., Gunsalus, R. P., & Dickerson, R. E. (1996) Biochemistry 35, 11053-11061.
4. Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495.
5. Bellsolell, L., Cronet, P., Majolero, M., Serrano, L., & Coll, M. (1996) J. Mol. Biol. 257, 116-128.
6. Brünger, A. T. (1992) X-PLOR Version 3.1, Yale University, New Haven, CT.
7. Burbulys, D., Trach, K. A., & Hoch, J. A. (1991) Cell 64, 545-552.
8. Clapham, D. E. (1995) Cell 80, 259-268.
9. Drake, S. K., Bourret, R. B., Luck, L. A., Simon, M. I., & Falke, J. J. (1993) J. Biol. Chem. 268, 13081-13088.
10. Evans, S. V. (1993) J. Mol. Graphics 11, 134-138.
11. Feher, V. A., Zapf, J. W., Hoch, J. A., Dahlquist, F. W., Whiteley, J. M., & Cavanagh, J. (1995) Protein Sci. 4, 1801-1814.
12. Ganguli, S., Wang, H., Matsumura, P., & Volz, K. (1995) J. Biol. Chem. 270, 17386-17393.
13. Grimsley, J. K., Tjalkens, R. B., Strauch, M. A., Bird, T. H., Spiegelman, G. B., Hostomsky, Z., Whiteley, J. M., & Hoch, J. A. (1994) J. Biol. Chem. 269, 16977-16982.
14. Hoch, J. A. (1993) Annu. Rev. Microbiol. 47, 441-465.
15. Howard, A. J., Nielsen, C., & Xuong, N. H. (1985) Methods Enzymol. 114, 452-472.
16. Kunkel, T. A., Roberts, J. D., & Zakour, R. A. (1987) Methods Enzymol. 154, 367-382.
17. Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
18. Lukat, G. S., Stock, A. M., & Stock, J. B. (1990) Biochemistry 29, 5436-5442.
19. Lukat, G. S., Lee, B. H., Mottonen, J. M., Stock, A. M., & Stock, J. B. (1991) J. Biol. Chem. 266, 8348-8354.
20. Madhusudan, Zapf, J., Whiteley, J. M., Hoch, J. A., Xuong, N. H., & Varughese, K. I. (1996a) Acta Crystallogr. D 52, 589-590.
21. Madhusudan, Zapf, J., Whiteley, J. M., Hoch, J. A., Xuong, N. H., & Varughese, K. I. (1996b) Structure 4, 679-690.
22. Moy, F. J., Lowry, D. F., Matsumura, P., Dahlquist, F. W., Krywko, J. E., & Domaille, P. J. (1994) Biochemistry 33, 10731-10742.
23. Needham, J. V., Chen, T. Y., & Falke, J. J. (1993) Biochemistry 32, 3363-3367.
24. Nicholls, A., Sharp, K. A., & Honig, B. (1991) Proteins 11, 281-296.
25. Norris, V., Chen, M., Goldberg, M., Voskuil, J., McGurk, G., & Holland, I. B. (1991) Mol. Microbiol. 5, 775-778.
26. Parkinson, J. S., & Kofoid, E. C. (1992) Annu. Rev. Genet. 26, 71-112.
27. Perego, M., & Hoch, J. A. (1996) Trends Genet. 12, 97-101.
28. Perego, M., Hanstein, C., Welsh, K. M., Djavakhishvili, T., Glaser, P., & Hoch, J. A. (1994) Cell 79, 1047-1055.
29. Roychoudhury, S., Zeilinski, N. A., Ninfa, A. J., Allen, N. E., Jungheim, L. N., Nicas, T. I., & Chakrabarty, A. M. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 965-969.
30. Santoro, J., Bruix, M., Pascual, J., Lopez, E., Serrano, L., & Rico, M. (1995) J. Mol. Biol. 247, 717-725.
31. Service, R. F. (1995) Science 270, 724-727.
32. Stock, A. M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749.
33. Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380.
34. Stock, J. B., Stock, A. M., & Mottonen, J. M. (1990) Nature 344, 395-400.
35. Swanson, R. V., Alex, L. A., & Simon, M. I. (1994) Trends Biochem. Sci. 19, 485-490.
36. Tisa, L. S., & Adler, J. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 11804-11808.
37. Tisa, L. S., & Adler, J. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 10777-10781.
38. Volkman, B. F., Nohaile, M. J., Amy, N. K., Kustu, S., & Wemmer, D. E. (1995) Biochemistry 34, 1413-1424.
39. Volz, K. (1993) Biochemistry 32, 11741-11753.
40. Volz, K. (1995) in Two-Component Signal Transduction (Hoch, J. A., & Silhavy, T. J., Eds.) pp 53-64, ASM Press, Washington, DC.
41. Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 266, 15511-15519.
42. Ward, L. D. (1985) Methods Enzymol. 117, 400.
43. Welch, M., Oosawa, K., Aizawa, S. I., & Eisenbach, M. (1994) Biochemistry 33, 10470-10476.
44. Zapf, J. W., Hoch, J. A., & Whiteley, J. M. (1996) Biochemistry 35, 2926-2933.