Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248

Biochemistry

Volumn 37, Issue 47, 1998, Pages 16555-16564

  Bukrinsky, Jens Thostrup ^b   Bjerrum, Morten Jannik ^b   Kadziola, Anders ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE A; ISOLEUCINE; TYROSINE; ZINC ION;

ARTICLE; CATTLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

ANIMALS; BINDING SITES; BINDING, COMPETITIVE; CARBOXYPEPTIDASES; CARBOXYPEPTIDASES A; CATTLE; COMPUTER SIMULATION; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN CONFORMATION; TYROSINE; ZINC;

EID: 0001357296     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981678i     Document Type: Article

References (64)

1. Rees, D. C., Lewis, M., and Lipscomb, W. N. (1983) J. Mol. Biol. 168, 367-387.
2. Sampath Kumar, K. S. V., Clegg, J. B., and Walsh, K. A. (1964) Biochemistry 3, 1728-1732.
3. Bargetzi, J.-P., Thompson, E. O. P., Sampath Kumar, K. S. V., Walsh, K. A., and Neurath, H. (1964) J. Biol. Chem. 239, 3767-3774.
4. Sampath Kumar, K. S. V., and Walsh, K. A. (1964) Biochemistry 3, 1726-1728.
5. Pétra, P. H., Bradshaw, R. A., Walsh, K. A., and Neurath, H. (1969) Biochemistry 8, 2762-2768.
6. Pétra, P. H., and Neurath, H. (1969) Biochemistry 8, 5029-5036.
7. Neurath, H., Bradshaw, R. A., Pétra, P. H., and Walsh, K. A. (1970) Philos. Trans. R. Soc. London B 257, 159-176.
8. Christianson, D. W., and Lipscomb, W. N. (1989) Acc. Chem. Res. 22, 62-69.
9. Makinen, M. W., Kuo, L. C., Dymowski, J. J., and Jaffer, S. (1979) J. Biol. Chem. 254, 356-366.
10. Kuo, L. C., and Makinen, M. W. (1982) J. Biol. Chem. 257, 24-27.
11. Christianson, D. W., Kuo, L. C., and Lipscomb, W. N. (1985) J. Am. Chem. Soc. 107, 8281-8283.
12. Christianson, D. W., and Lipscomb, W. N. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 6840-6844.
13. Christianson, D. W., and Lipscomb, W. N. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7568-7572.
14. Christianson, D. W., and Lipscomb, W. N. (1986) J. Am. Chem. Soc. 108, 545-546.
15. Christianson, D. W., and Lipscomb, W. N. (1986) J. Am. Chem. Soc. 108, 4998-5003.
16. Christianson, D. W., David, P. R., and Lipscomb, W. N. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 1512-1515.
17. Christianson, D. W., and Lipscomb, W. N. (1987) J. Am. Chem. Soc. 109, 5536-5538.
18. Christianson, D. W., and Lipscomb, W. N. (1988) J. Am. Chem. Soc. 110, 5560-5565.
19. Lipscomb, W. N., Hartsuck, J. A., Reeke, G. N., Quiocho, F. A., Bethge, P. H., Ludwig, M. L., Steitz, T. A., Muirhead, H., and Coppola, J. C. (1968) Brookhaven Symp. Biol. 21, 24-90.
20. Lipscomb, W. N., Reeke, G. N., Hartsuck, J. A., Quiocho, F. A., and Bethge, P. H. (1970) Philos. Trans. R. Soc. London B 257, 177-214.
21. Mangani, S., Carloni, P., and Orioli, P. (1992) J. Mol. Biol. 223, 573-578.
22. Rees, D. C., and Lipscomb, W. N. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 5455-5459.
23. Rees, D. C., and Lipscomb, W. N. (1982) J. Mol. Biol. 160, 475-498.
24. Rees, D. C., and Lipscomb, W. N. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 7151-7154.
25. Shoham, G., Rees, D. C., and Lipscomb, W. N. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 7767-7771.
26. Shoham, G., Christianson, D. W., and Oren, D. A. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 684-688.
27. Greenblatt, H. M., Feinberg, H., Tucker, P. A., and Shoham, G. (1998) Acta Crystallogr., Sect. D 54, 289-305.
28. Gomez-Ortiz, M., Gomis-Rüth, F. X., Huber, R., and Avilés, F. X. (1997) FEBS Lett. 400, 336-340.
29. Larsen, K. S., and Auld, D. S. (1991) Biochemistry 30, 2613-2618.
30. Cox, D. J., Bovard, F. C., Bargetzi, J.-P., Walsh, K. A., and Neurath, H. (1964) Biochemistry 3, 44-47.
31. Lipscomb, W. N., Coppola, J. C., Hartsuck, J. A., Ludwig, M. L., Muirhead, H., Searl, J., and Steitz, T. A. (1966) J. Mol. Biol. 19, 423-441.
32. Bargetzi, J.-P., Sampath Kumar, K. S. V., Cox, D. J., Walsh, K. A., and Neurath, H. (1963) Biochemistry 2, 1468-1474.
33. Gewirth, D. (1995) The HKL Manual: an Oscillation Data Processing Suite for Macromolecular Crystallography. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven CT.
34. Navaza, J. (1991) Acta Crystallogr., Sect. D 49, 588-591.
35. Brünger, A. T. (1992) X-PLOR, version 3.1: A System for X-ray Crystallography and NMR. Yale University, New Haven CT.
36. Engh, R. A., and Huber, R. (1991) Acta Crystallogr., Sect. A 47, 392-400.
37. Le Huërou, I., Guilloteau, P., Toullec, R., Puigserver, A., and Wicker, C. (1991) Biochem. Biophys. Res. Commun. 175, 110-116.
38. Roussel, A, and Cambillau, C. (1992) TURBO-FRODO, Biographics and AFMB (Architecture et Fonction des Macromolécules Biologiques), Marseille, France.
39. Read, R. J. (1986) Acta Crystallogr., Sect. A 42, 140-149.
40. Collaborative Computational Project no. 4 (1994) Acta Crystallogr., Sect. D 50, 760-763.
41. Kraut, J. (1968) J. Mol. Biol. 35, 511-512.
42. International Tables for Crystallography Vol. C: Mathematical, Physical and Chemical Tables (1992) (Wilson, A. J. C., Ed.) pp 219-222, Kluwer Academic Publishers, London.
43. Laursen, J. (1985) Colloquium Spectroscopicum Internationale XXIV 1, 38-39.
44. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497.
45. Larsen, K. S., and Auld, D. S. (1989) Biochemistry 28, 9620-9625.
46. Brünger, A. T. (1992) Nature 355, 472-475.
47. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
48. Koshland, D. E. (1958) Proc. Natl. Acad. Sci. U.S.A. 44, 98-104.
49. Simpson, R. T., Riordan, J. F., and Vallee, B. L. (1963) Biochemistry 2, 616-622.
50. Johansen, J. T., and Vallee, B. L. (1971) Proc. Natl. Acad. Sci. U.S.A. 68, 2532-2535.
51. Johansen, J. T., and Vallee, B. L. (1973) Proc. Natl. Acad. Sci. U.S.A. 70, 2006-2010.
52. Johansen, J. T., and Vallee, B. L. (1975) Biochemistry 14, 649-660.
53. Riordan, J. F., and Muszynska, G. (1974) Biochem. Biophys. Res. Commun. 57, 447-451.
54. Spilburg, C. A., Bethune, J. L., and Vallee, B. L. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 3922-3926.
55. Scheule, R. K., Van Wart, H. E., Vallee, B. L., and Scheraga, H. A. (1980) Biochemistry 19, 759-766.
56. Bachovchin, W. W., Kanamori, K., Vallee, B. L., and Roberts, J. D. (1982) Biochemistry 21, 2885-2892.
57. Bauer, R., Bjerrum, M., Danielsen, E., Friis, E., Hammerstad, J. M., Hemmingsen, L., Pedersen, M. V., and Ulstrup, J. (1996) in Protein Folds (Bohr, H., and Brunak, S., Eds.) pp 31-42, CRC Press, New York.
58. Bauer, R., Danielsen, E., Hemmingsen, L., Sørensen, M. V., Ulstrup, J., Friis, E. P., Auld, D. S., and Bjerrum, M. J. (1997) Biochemistry 36, 11514-11524.
59. Gardell, S. J., Craik, C. S., Hilvert, D., Urdea, M. S., and Rutter, W. J. (1985) Nature 317, 551-555.
60. Hilvert D., Gardell, S. J., Rutter, W. J., and Kaiser, E. T. (1986) J. Am. Chem. Soc. 108, 5298-5304.
61. Williams, A. C., and Auld, D. S. (1986) Biochemistry 25, 94-100.
62. Teplyakov, A., Polyakov, K., Obmolova, G., Strokopytov, B., Kuranova, I., Osterman, A., Grishin, N., Smulevitch, S., Zagnitko, O., Galperina, O., Matz, M., and Stepanov, V. (1992) Eur. J. Biochem. 208, 281-288.
63. Qian, M., Haser, R., and Payan, F. (1993) J. Mol. Biol. 231, 785-799.
64. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.