Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker

Biochemistry

Volumn 35, Issue 2, 1996, Pages 433-443

  Zhou, Hongjun ^a   McEvoy, Megan M ^a   Lowry, David F ^a   Swanson, Ronald V ^b,c   Simon, Melvin I ^b   Dahlquist, Frederick W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^c Recombinant BioCatalysis Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HISTIDINE AUTOKINASE; NITROGEN 15; PHOSPHORUS; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; DYNAMICS; ENZYME ANALYSIS; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; ESCHERICHIA COLI; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 0030043573     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi951960e     Document Type: Article

References (52)

1. Barbato, G., Ikura, M., Kay, L. E., Paster, R. W., & Bax, A. (1992) Biochemistry 31, 5269-5278.
2. Billeter, M., Neri, D., Otting, G., Qian, Y. Q., & Wüthrich, K. (1992) J. Biomol. NMR 2, 257-274.
3. Bodenhausen, G., Kogler, H., & Ernst, R. R. (1984) J. Magn. Reson. 58, 5485-5489.
4. Borkovich, K. A., & Simon, M. I. (1990) Cell 63, 1339-1348.
5. Borkovich, K. A., Kaplan, N., Hess, J. F., & Simon, M. I. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 1208-1212.
6. Borkovich, K. A., Alex, L. A., & Simon, M. I. (1992) Proc. Natl Acad. Sci. U.S.A. 89, 6756-6760.
7. Bourret, R. B., Borkovich, K. A., & Simon, M. I. (1991) Annu. Rev. Biochem. 60, 401-441.
8. Cantor, C. R., & Schimmel, P. R. (1980) Biophysical Chemistry, W. H. Freeman and Co., New York.
9. Cavanagh, J., Chazin, W. J., & Rance, M. (1989) J. Magn. Reson. 87, 110-131.
10. Clore, G. M., Driscoll, P. C., Wingfield, P. T., & Gronenborn, A. M. (1990) Biochemistry 29, 7387-7401.
11. Englander, S. W., & Wand, A. J. (1987) Biochemistry 26, 5953-5958.
12. Garrett, D. G., Powers, R., March, C. J., Frieden, E. A., Clore, G. M., & Gronenborn, A. M. (1992) Biochemistry 31, 4547-4553.
13. Gegner, J. A., Graham, D. R., Roth, A. F., & Dahlquist, F. W. (1992) Cell 70, 975-982.
14. Hansen, A. P., Petros, A. M., Meadows, R. P., & Fesik, S. W. (1994) Biochemistry 33, 15418-15424.
15. Hess, J. F., Oosawa, K., Kaplan, N., & Simon, M. I. (1988a) Cell 53, 79-87.
16. Hess, J. F., Bourret, R. B., & Simon, M. I. (1988b) Nature 336, 139-143.
17. Huntress, W. T. (1968) J. Chem. Phys. 48, 3524-3533.
18. Kay, L. E., & Bax, A. (1990) J. Magn. Reson. 86, 110-126.
19. Kay, L. E., Torchia, D. A., & Bax, A. (1989a) Biochemistry 28, 8972-8979.
20. Kay, L. E., Marion, D., & Bax, A. (1989b) J. Magn. Reson. 84, 72-84.
21. Karplus, M. (1995) J. Phys. Chem. 30, 11-15.
22. Kumar, A., Wüthrich, K., & Ernst, R. R. (1980) Biochem. Biophys. Res. Commun. 95, 1-6.
23. Lipari, G., & Szabo, A. (1992) J. Am. Chem. Soc. 104, 4546-4558.
24. Lupas, A., & Stock, J. (1989) J. Biol. Chem. 264, 17337-17342.
25. Macura, S., & Ernst, R. R. (1980) Mol. Phys. 41, 95-117.
26. Marion, D., Ikura, M., Tschudin, R., & Bax, A. (1989) J. Magn. Reson. 85, 393-399.
27. McEvoy, M. M., Zhou, H., Roth, A. F., Lowry, D. L., Morrison, T. B., Kay, L. E., & Dahlquist, F. W. (1995) Biochemistry 34, 13871-13880.
28. McNally, D. F., & Matsumura, P. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 6269-6273.
29. Milburn, M. V., Privé, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E., & Kim, S.-H. (1991) Science 254, 1342-1347.
30. Morrison, T., & Parkinson, J. S. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 5485-5489.
31. Ninfa, E. G., Stock, A., Mowbray, S., & Stock, J. (1991) J. Biol. Chem. 266, 9764-9770.
32. Nowak, U. K., Li, A., Teuten, A. J., Smith, R. A. G., & Dobson, C. M. (1993) Biochemistry 32, 298-309.
33. Parkinson, J. S., & Kofoid, E. C. (1992) Annu. Rev. Genet. 26, 71-112.
34. Presnell, S. R., & Cohen, F. E. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6592-6596.
35. Press. W. H., Teukolsky, S. A., Vetterling, W. T., & Hannery, B. P. (1992) Numerical Recipes. Cambridge University Press, England.
36. Roman, S. J., Meyers, M., Voltz, K., & Matsumura, P. (1992) J. Bacteriol. 174, 6247-6255.
37. Sanders, D. A., Gillece-Castro, B. L., Stock, A. M., Burlingame, A. L., & Koshland, D. E., Jr. (1989) J. Biol. Chem. 264, 21770-21778.
38. Smith, R. A., & Parkinson, J. S. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 5370-5374.
39. Stewart, R. C., & Dahlquist, F. W. (1987) Chem. Rev. 87, 997-1025.
40. Stock, A. M., Wylie, D. C., Mottonen, J. M., Lupas, A. N., Ninfa, E. G., Ninfa, A. J., Schutt, C. E., & Stock, J. B. (1988) Cold Spring Harbor Symp. Quant. Biol. 53, 49-57.
41. Stock, J. B., Ninfa, A. J., & Stock, A. M. (1989) Microbiol. Rev. 53, 450-490.
42. Stock, J. B., Lukat, G. S., & Stock, A. M. (1991) Annu. Rev. Biophys. Biophys. Chem. 20, 109-136.
43. Swanson, R. V., Schuster, S. C., & Simon, M. I. (1993) Biochemistry 32, 7623-7629.
44. Tjandra, N., Kuboniwa, H., Ren, H., & Bax, A. (1995) Eur. J. Biochem. 230, 1014-1024.
45. Woessner, D. T. (1962) J. Chem. Phys. 37, 647-654.
46. Wolfe, A. J., & Stewart, R. C. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 1518-1522.
47. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.
48. Wylie, D., Stock, A., Wong, C.-Y., & Stock, J. (1988) Biochem. Biophys. Res. Commun. 151, 891-896.
49. Zhou, H., Lowry, D. F., Swanson, R. V., Simon, M. I. & Dahlquist, F. W. (1995) Biochemistry 34, 13858-13870.
50. Zuiderweg, E. R. P. (1990) J. Magn. Reson. 86, 346-357.
51. Zuiderweg, E. R. P., & Fesik, S. W. (1989) Biochemistry 28, 2387-2391.
52. Zuidenweg, E. R. P., Hallenga, K., & Olejniczak, E. T. (1986) J. Magn. Reson. 70, 336-343.