Backbone dynamics of Escherichia coli adenylate kinase at the extreme stages of the catalytic cycle studied by 15N NMR relaxation

Biochemistry

Volumn 39, Issue 22, 2000, Pages 6634-6644

  Shapiro, Yury E ^a   Sinev, Michael A ^a   Sineva, Elena V ^a   Tugarinov, Vitali ^b   Meirovitch, Eva ^a  

^a BAR ILAN UNIVERSITY   (Israel)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE;

ANISOTROPY; ARTICLE; CATALYSIS; CRYSTALLOGRAPHY; DIFFUSION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; THERMODYNAMICS;

ADENYLATE KINASE; DIFFUSION; DINUCLEOSIDE PHOSPHATES; ENZYME INHIBITORS; ESCHERICHIA COLI; HYDROGEN BONDING; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034612241     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992076h     Document Type: Article

References (71)

1. Bennett, W. S., and Huber, R. (1984) Crit. Rev. Biochem. 15, 291-384.
2. Sicheri, F., and Kuriyan, J. (1997) Curr. Opin. Struct. Biol. 7, 777-785.
3. Mayer, B. J., Hirai, H., and Sakai, R. (1995) Curr. Biol. 5, 296-305.
4. Cambell, I. D., and Downing, A. K. (1998) Nat. Struct. Biol. 5 (Suppl.), 496-499.
5. Fushman, D., Xu, R., and Cowburn, D. (1999) Biochemistry 38, 10225-10230.
6. Gerstein, M., Lesk, A. M., and Chothia, C. (1994) Biochemistry 33, 6739-6749.
7. Noda, L. (1973) in The Enzymes (Boyer, P. D., Ed.) Vol. 8, pp 279-305.
8. Vornhein, C., Schlauderer, G. J., and Schulz, G. (1995) Structure 3, 483-490.
9. Müller, C. W., and Schulz, G. (1992) J. Mol. Biol. 224, 159-177.
10. Müller, C. W., Schlauderer, G. J., Reinstein, J., and Schulz, G. (1996) Structure 4, 147-156.
11. Anderson, C. M., Zucker, F. H., and Steiz, T. A. (1979) Science 204, 375-380.
12. Berry, M. B., Meador, B., Bilderback, T., Liang, P., and Glaser, M. (1994) Proteins: Struct., Funct., Genet. 19, 183-198.
13. Schulz, G., Müller, C. W., and Deiderichs, K. (1990) J. Mol. Biol. 213, 627-630.
14. Müller-Dickermann, H.-J., and Schulz, G. E. (1995) J. Mol. Biol. 246, 522-530.
15. Richard, J. P., and Frey, P. A. (1978) J. Am. Chem. Soc. 100, 7757-7758.
16. Sinev, M. A., Sineva, E. V., Ittah, V., and Haas, E. (1996) Biochemistry 35, 6425-6437.
17. Sinev, M. A., Sineva, E. V., Ittah, V., and Haas, E. (1996) FEBS Lett. 397, 273-276.
18. Vetter, I., Konrad, M., and Rosch, P. (1991) Biochemistry 30, 4137-4142 and references therein.
19. Byeon, I.-J., Yan, H., Edison, A. S., Mooberry, E. S., Abildgaard, F., Markley, J. L., and Tsai, M.-D. (1993) Biochemistry 32, 12508-12521.
20. Byeon, I.-J., Shi, Z., and Tsai, M.-D. (1995) Biochemistry 34, 3172-3182.
21. Burlacu-Miron, S., Perrier, V., Gilles, A.-M., Pistotnik, E., and Craescu, C. T. (1998) J. Biol. Chem. 273, 19102-19107.
22. Burlacu-Miron, S., Perrier, V., Gilles, A.-M., Mispelter, J., Barzu, O., and Craescu, C. T. (1999) J. Biomol. NMR 13, 93-94.
23. Burlacu-Miron, S., Gilles, A. M., Popescu, A., Barzu, O., and Craescu, C. T. (1999) Eur. J. Biochem. 264, 765-774.
24. Peng, J. W., and Wagner, G. (1994) in Methods in Enzymology (James, T. L., and Oppenheimer, N. J., Eds.) Vol. 239, pp 563-595, Academic Press, New York.
25. Abragam, A. (1961) Principles of Nuclear Magnetism, Oxford University Press, London.
26. Bloom, M., Reeves, L. W., and Wells, E. J. (1965) J. Chem. Phys. 42, 1615-1625.
27. Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546-4559.
28. Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4559-4570.
29. Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. (1990) J. Am. Chem. Soc. 112, 4989-4991.
30. Clore, G. M., Driscoll, P. C., Wingfield, P. T., and Gronenborn, A. (1990) Biochemistry 29, 7387-7401.
31. Tjandra, N., Feller, S. E., Pastor, R. W., and Bax, A. (1995) J. Am. Chem. Soc. 117, 12562-12566.
32. Zheng, Z., Czaplicki, J., and Jardetzky, O. (1995) Biochemistry 34, 5212-5223.
33. Brüschweiler, R., Liao, X., and Wright, P. E. (1995) Science 268, 886-889.
34. Lee, L. K., Rance, M., Chazin, W. J., and Palmer, A. G., III (1997) J. Biomol. NMR 9, 287-298.
35. Reinstein, J., Brunne, M., and Wittinghofer, A. (1988) Biochemistry 27, 4712-4720.
36. Girons, I. S., Gilles, A.-M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A., and Barzu, O. (1987) J. Biol. Chem. 262, 622-629.
37. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293.
38. Void, R. L., Waugh, J. S., Klein, M. P., and Phelps, D. E. (1968) J. Chem. Phys. 48, 3831-3832.
39. Meiboom, S., and Gill, D. (1958) Rev. Sci. Instrum. 29, 688-691.
40. Noggle, J. H., and Shirmer, R. E. (1971) The Nuclear Overhauser Effect: Chemical Aplications, Academic Press, New York.
41. Kay, L. E., Nicholson, L. K., Delaglio, F., Bax, A., and Torchia, D. A. (1992) J. Magn. Reson. 97, 359-375.
42. Palmer, A. G., III, Skelton, N. J., Chazin, W. J., Wright, P. E., and Rance, M. (1992) Mol. Phys. 75, 699-711.
43. Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12593-12594.
44. Tjandra, N., Szabo, A., and Bax, A. (1996) J. Am. Chem. Soc. 118, 6986-6991.
45. Live, D. H., Davis, D. G., Agosta, W. C., and Cowburn, D. (1984) J. Am. Chem. Soc. 106, 1939-1941.
46. Palmer, A. G., III, Rance, M., and Wright, P. E. (1991) J. Am. Chem. Soc. 113, 4371-4380.
47. Br̈nger, A. T. (1992) X-PLOR, Version 3.1. A System for X-ray Crystallography and NMR, Yale University Press, New Haven, CT.
48. Hyiama, Y., Niu, C. H., Silverton, J. V., Bavaso, A., and Torchia, D. A. (1988) J. Am. Chem. Soc. 110, 2378-2383.
49. Fushman, D., Tjandra, N., and Cowburn, D. (1998) J. Am. Chem. Soc. 120, 10947-10952.
50. Fushman, D., and Cowburn, D (1999) J. Biomol. NMR 13, 139-147.
51. Kroenke, C. D., Rance, M., and Palmer, A. G., III (1999) J. Am. Chem. Soc. 121, 10119-10125.
52. Mandel, A. M., Akke, M., and Palmer, A. G., III (1995) J. Mol. Biol. 246, 144-163.
53. Bodenhausen, G., and Ruben, D. J. (1980) Chem. Phys. Lett. 69, 185-189.
54. Marion, D., Driscoll, P. C., Kay, L. E., Wingfield, P. T., Bax, A., Gronenborn, A. M., and Clore, G. M. (1989) Biochemistry 28, 6150-6156.
55. Marion, D., Kay, L. E., Sparks, S. W., Torchia, D. A., and Bax, A. (1989) J. Am. Chem. Soc. 111, 1515-1517.
56. Zuiderweg, E. R. P., and Fesik, S. W. (1989) Biochemistry 28, 2387-2391.
57. Vuister, G. W., and Bax, A. (1993) J. Am. Chem. Soc. 115, 7772-7777.
58. Meirovitch, E., Sinev, M. A., and Sineva, E. V. (1999) J. Biomol. NMR 13, 195-196.
59. Zhang, P., Dayie, K., and Wagner, G. (1997) J. Mol. Biol. 272, 443-455.
60. Yao, S., Hinds, M. G., and Norton, R. S. (1998) J. Magn. Reson. 131, 347-350.
61. Shapiro, Yu. E., Gorbatyuk, V. Ya., Levashov, A. V., and Klyachko, N. L. (1994) Biol. Membr. 7, 277-290.
62. Copie, V., Tomita, Y., Akiyama, S. K., Aota, A., Yamada, K. M., Venable, R. M., Pastor, R. W., Krueger, S., and Torchia, D. A. (1998) J. Mol. Biol 277, 663-682.
63. Wagner, G. (1997) Nat. Struct. Biol. 5 (Suppl.), 841-844.
64. Fushman, D., Cahill, S., and Cowburn. D. (1997) J. Mol. Biol. 266, 173-194.
65. De Alba, E., Baber, J. L., and Tjandra, N. (1999) J. Am. Chem. Soc. 121, 4281-4283.
66. Korzhnev, D. M., Orekhov, V. Y., and Arseniev, A. S. (1997) J. Magn. Reson. 127, 184-191.
67. Fushman, D., and Cowburn, D. (1998) J. Am. Chem. Soc. 120, 7109-7110.
68. Carr, P. A., Erickson, H. P., and Palmer, A. G., III (1997) Structure 5, 949-959.
69. Nicholson, L. K., Yamazaki, T., Torcia, D. A., Grzesiek, S., Bax, A., Stahl, S. J., Kaufman, J. D., Wingfield, P. T., Lam, P. Y. S., Jadhav, P. K., Hodge. C. N., Domaille, P. J., and Chang, C.-H. (1995) Struct. Biol. 2, 274-279.
70. Berry, M. B., and Phillips, G. N. (1988) Proteins: Struct., Fund., Genet. 32, 276-288.
71. Kraulis, P. J. (1991) Molscript: A Program to Produce both Detailed and Schematic Plots of Protein Structures. J. Appl. Crystallogr. 24, 946-995.