Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1

Biochemistry

Volumn 37, Issue 46, 1998, Pages 16192-16200

  Hebert, Eric J ^a   Giletto, Anthony ^a   Sevcik, Jozef ^b   Urbanikova, Lubica ^b   Wilson, Keith S ^c   Dauter, Zbigniew ^c   Pace, C Nick ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b INSTITUTE OF CHEMISTRY   (Slovakia)

^c UNIVERSITY OF YORK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMIDE; ASPARAGINE; ASPARTIC ACID; GLOBULAR PROTEIN; HYDROGEN; MUTANT PROTEIN; PEPTIDE; RIBONUCLEASE; SERINE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME STABILITY; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL;

ASPARAGINE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; HYDROGEN BONDING; ISOENZYMES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE T1; RIBONUCLEASES; SERINE; UREA;

EID: 0032542062     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9815243     Document Type: Article

References (77)

1. Wolfenden, R. (1978) Biochemistry 17, 201-204.
2. Lesser, G. J., and Rose, G. D. (1990) Proteins: Struct., Funct., Genet. 8, 6-13.
3. Stickle, D. F., Presta, L. G., Dill, K. A., and Rose, G. D. (1992) J. Mol. Biol. 226, 1143-1159.
4. Lu, W., Qasim, M. A., Laskowski, M. J., and Kent, S. B. (1997) Biochemistry 36, 673-679.
5. Koh, J. T., Cornish, V. W., and Schultz, P. G. (1997) Biochemistry 36, 11314-11322.
6. Eberhardt, E. S., Wittmayer, P. K., Templer, B. M., and Raines, Biophys. Acta 235, 335-342.
7. Hebert, E. J., Grimsley, G. R., Hartley, R. W., Horn, G., Schell, D., Garcia, S., Both, V., Sevcik, J., and Pace, C. N. (1997) Protein Expression Purif. 11, 162-168.
8. Pace, C. N., Hebert, E. J., Shaw, K. L., Schell, D., Both, V., Krajcikova, D., Sevcik, J., Wilson, K. S., Dauter, Z., Hartley, R. W., and Grimsley, G. R. (1998) J. Mol. Biol. 279, 271-286.
9. Hill, C. P., Dodson, G. G., Heinemann, U., Saenger, W., Mitsui, Y., Nakamura, K. T., Borisov, S., Tischenko, G., Polyakov, K. M., and Pavlovsky, S. (1983) Trends Biochem. Sci. 8, 364-369.
10. Hartley, R. W. (1997) in Ribonucleases structures and functions (D'Alessio, G., and Riordan, J. F., Eds.) pp 51-100, Academic Press, Inc., New York.
11. Johnson, C. M., Oliveberg, M., Clarke, J., and Fersht, A. R. (1997) J. Mol. Biol. 268, 198-208.
12. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1997) Biochemistry 36, 10923-10929.
13. Mayr, L. M., Odefey, C., Schutkowski, M., and Schmid, F. X. (1996) Biochemistry 35, 5550-5561.
14. Sevcik, J., Sanishvili, R. G., Pavlovsky, A. G., and Polyakov, K. M. (1990) Trends Biochem. Sci. 15, 158-162.
15. Serrano, L., Kellis, J. T., Cann, P., Matouschek, A., and Fersht, A. R. (1992) J. Mol. Biol. 224, 783-804.
16. Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Gene 77, 51-59.
17. Shirley, B. A., Stanssens, P., Hahn, U., and Pace, C. N. (1992) Biochemistry 31, 725-732.
18. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 2833-2837.
19. Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. R., and Gray, T. (1995) Protein Sci. 4, 2411-2423.
20. Santoro, M. M., and Bolen, D. W. (1992) Biochemistry 31, 4901-4907.
21. Pace, C. N., and Scholtz, J. M. (1997) in Protein structure: a practical approach (Creighton, T. E., Ed.) pp 299-321, Oxford University Press, New York.
22. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326.
23. Navaza, J., and Saludjian, P. (1997) Methods Enzymol. 276, 581-619.
24. Sevcik, J., Dauter, Z., Lamzin, V. S., and Wilson, K. S. (1996) Acta Crystallogr. 52, 327-344.
25. Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. F. J., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., and Tasumi, M. (1977) Eur. J. Biochem. 80, 319-324.
26. Murshudov, G., Vagin, A., and Dodson, E. J. (1997) Acta Crystallogr. D53, 240-255.
27. Lamzin, V. S., and Wilson, K. S. (1997) Methods Enzymol. 277, 269-305.
28. Brunger, A. T. (1992) Nature 355, 472-475.
29. Lee, B., and Richards, F. M. (1971) J. Mol. Biol. 55, 379-400.
30. Richards, F. M. (1977) Annu. Rev. Biophys. Biophys. Chem. 6, 151-176.
31. Baker, E. N., and Hubbard, R. E. (1984) Prog. Biophys. Mol. Biol. 44, 97-179.
32. Ippolito, J. A., Alexander, R. S., and Christianson, D. W. (1990) J. Mol. Biol. 215, 457-471.
33. Presta, L. G., and Rose, G. D. (1988) Science 240, 1632-1640.
34. McDonald, I. K., and Thornton, J. M. (1994) J. Mol. Biol. 238, 777-793.
35. Thomson, J. A., Shirley, B. A., Grimsley, G. R., and Pace, C. N. (1989) J. Biol. Chem. 264, 11614-11620.
36. Greene, R. F. J., and Pace, C. N. (1974) J. Biol. Chem. 249, 5388-5393.
37. Pace, C. N. (1986) Methods Enzymol. 131, 266-280.
38. Stites, W. E., Gittis, A. G., Lattman, E. E., and Shortle, D. (1991) J. Mol. Biol. 221, 7-14.
39. Walter, S., Hubner, B., Hahn, U., and Schmid, F. X. (1995) J. Mol. Biol. 252, 133-143.
40. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
41. Privalov, P. L., Tiktopulo, E. I., Venyaminov S. Y., Griko, Y. V., Makhatadze, G. I., and Khechinashvili, N. N. (1989) J. Mol. Biol. 205, 737-750.
42. Klapper, M. H. (1971) Biochim. Biophys. Acta 229, 557-566.
43. London, F. (1937) Trans. Faraday Soc. 33, 8-26.
44. Harpaz, Y., Gerstein, M., and Chothia, C. (1994) Structure 2, 641-649.
45. Pace, C. N. (1995) Methods Enzymol. 259, 538-554.
46. Myers, J. K., and Pace, C. N. (1996) Biophys. J. 71, 2033-2039.
47. Xu, J., Baase, W. A., Baldwin, E., and Matthews, B. W. (1998) Protein Sci. 7, 158-177.
48. Matthews, B. W. (1995) Adv. Protein Chem. 46, 249-279.
49. Irie, M. (1997) in Ribonucleases structures and functions (D'Alessio, G., and Riordan, J. F., Eds.) pp 101-130, Academic Press, Inc., New York.
50. Kim, K.-S., Tao, F., Fuchs, J. A., Danishefsky, A. T., Housset, D., Wlodawer, A., and Woodward, C. (1993) Protein Sci. 2, 588-596.
51. Fersht, A. R. (1988) Biochemistry 27, 1577-1580.
52. Nozaki, Y., and Tanford, C. (1967) J. Biol. Chem. 242, 4731-4735.
53. Nozaki, Y., and Tanford, C. (1967) Methods Enzymol. 11, 715.
54. Bundi, A., and Wuthrich, K. (1979) Biopolymers 18, 285-297.
55. Antosiewicz, J., McCammon, J. A., and Gilson, M. K. (1996) Biochemistry 35, 7819-7833.
56. Sippl, M. J., Ortner, M., Jaritz, M., Lackner, P., and Flockner, H. (1996) Folding Des. 1, 289-298.
57. Froloff, N., Windemuth, A., and Honig, B. (1997) Protein Sci. 6, 1293-1301.
58. Shan, S., and Herschlag, D. (1998) Methods Enzymol. (in press).
59. Fersht, A. R., Shi, J. P., Knill-Jones, J., Lowe, D. M., Wilkinson, A. J., Blow, D. M., Brick, P., Carter, P., Waye, M. M., and Winter, G. (1985) Nature 314, 235-238.
60. Milla, M. E., Brown, B. M., and Sauer, R. T. (1994) Nat. Struct. Biol. 1, 518-523.
61. Yamada, H., Kanaya, E., Ueno, Y., Ikehara, M., Nakamura, H., and Kikkuchi, M. (1994) Biol. Pharm. Bull. 17, 612-616.
62. Byrne, M. P., Manuel, R. L., Lowe, L. G., and Stites, W. E. (1995) Biochemistry 34, 13949-13960.
63. Makhatadze, G. I., and Privalov, P. L. (1995) Adv. Protein Chem. 47, 307-425.
64. Huyghues-Despointes, B. M. P., Klinger, T. M., and Baldwin, R. L. (1995) Biochemistry 34, 13267-13271.
65. Thorson, J. S., Chapman, E., and Schultz, P. G. (1995) J. Am. Chem. Soc. 117, 9361-9362.
66. Habermann, S. M., and Murphy, K. P. (1996) Protein Sci. 5, 1229-1239.
67. Ross, P. D., and Rekharsky, M. V. (1996) Biophys. J. 71, 2144-2154.
68. Chapman, E., Thorson, J. S., and Schultz, P. G. (1997) J. Am. Chem. Soc. 119, 7151-7152.
69. Honig, B., and Yang, A. S. (1995) Adv. Protein Chem. 46, 27-58.
70. Yang, A. S., and Honig, B. (1995) J. Mol. Biol. 252, 351-365.
71. Lazaridis, T., Archontis, G., and Karplus, M. (1995) Adv. Protein Chem. 47, 231-306.
72. Becktel, W. J., and Schellman, J. A. (1987) Biopolymers 26, 1859-1877.
73. Radzicka, A., and Wolfenden, R. (1988) Biochemistry 27, 1644-1670.
74. Fauchere, J. L., and Pliska, V. E. (1983) Eur. J. Med. Chem. 18, 369-375.
75. Goldenberg, D. P., Frieden, R. W., Haack, J. A., and Morrison, T. B. (1989) Nature 338, 127-132.
76. Green, S. M., Meeker, A. K., and Shortle, D. (1992) Biochemistry 31, 5717-5728.
77. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.