Removing the invariant salt bridge of parvalbumin increases flexibility in the AB-loop structure

Acta Crystallographica Section D: Biological Crystallography

Volumn 65, Issue 8, 2009, Pages 733-743

  Hoh, François ^a   Cavé, Adrien ^a   Strub, Marie Paule ^b   Banres, Jean Louis ^c   Padilla, André ^a  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c CNRS   (France)

Author keywords

Calcium binding proteins; EF hands; Flexibility; Parvalbumin

Indexed keywords

CALCIUM; MAGNESIUM; MUTANT PROTEIN; PARVALBUMIN;

ANIMAL; ARTICLE; BINDING SITE; CHEMISTRY; CRYSTALLIZATION; FISH; GENETICS; HUMAN; METABOLISM; MOUSE; PROTEIN BINDING; PROTEIN DATABASE; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STABILITY; RAT; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY; XENOPUS LAEVIS;

ANIMALS; BINDING SITES; CALCIUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DATABASES, PROTEIN; EF HAND MOTIFS; FISHES; HUMANS; MAGNESIUM; MICE; MUTANT PROTEINS; PARVALBUMINS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STABILITY; RATS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS LAEVIS;

RATTUS;

EID: 68349143058     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444909011482     Document Type: Article

References (64)

1. Agah, S., Larson, J. D. & Henzl, M. T. (2003). Biochemistry, 42, 10886-10895.
2. Alattia, T., Padilla, A. & Cavé, A. (1996). Eur. J. Biochem. 237, 561-574.
3. Baldellon, C., Alattia, J. R., Strub, M.-P., Pauls, T., Berchtold, M. W., Cavé, A. & Padilla, A. (1998). Biochemistry, 37, 9964-9975.
4. Baldellon, C., Padilla, A. & Cavé, A. (1992). Biochimie, 74, 837-844.
5. Bottoms, C. A., Schuermann, J. P., Agah, S., Henzl, M. T. & Tanner, J. J. (2004). Protein Sci. 13, 1724-1734.
6. Brünger, A. T. (1993). Acta Cryst. D49, 24-36.
7. Cates, M. S., Berry, M. B., Ho, E. L., Li, Q., Potter, J. D. & Phillips, G. N. Jr (1999). Structure, 7, 1269-1278.
8. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
9. Cox, J. A., Milos, M. & MacManus, J. P. (1990). J. Biol. Chem. 265, 6633-6637.
10. da Silva, A. C. & Reinach, F. C. (1991). Trends Biochem. Sci. 16, 53-57.
11. Dong, F., Vijayakumar, M. & Zhou, H. X. (2003). Biophys. J. 85, 49-60.
12. Drake, S. K. & Falke, J. J. (1996). Biochemistry, 35, 1753-1760.
13. Drake, S. K., Zimmer, M. A., Miller, C. L. & Falke, J. J. (1997). Biochemistry, 36, 9917-9926.
14. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
15. Gillen, M. F., Banville, D., Rutledge, R. G., Narang, S., Seligy, V. L., Whitfield, J. F. & MacManus, J. P. (1987). J. Biol. Chem. 262, 5308-5312.
16. Go, N., Noguti, T. & Nishikawa, T. (1983). Proc. Natl Acad. Sci. USA, 80, 3696-3700.
17. Golden, L. F., Corson, D. C., Sykes, B. D., Banville, D. & MacManus, J. P. (1989). J. Biol. Chem. 264, 20314-20319.
18. Goodman, M. & Pechere, J. F. (1977). J. Mol. Med. 9, 131-158.
19. Gosselin-Rey, C., Bernard, N. & Gerday, C. (1973). Biochim. Biophys. Acta, 303, 90-104.
20. Grove, A. (2003). Biochemistry, 42, 8739-8747.
21. Hapak, R. C., Lammers, P. J., Palmisano, W. A., Birnbaum, E. R. & Henzl, M. T. (1989). J. Biol. Chem. 264, 18751-18760.
22. Heizmann, C. W. (1984). Experientia, 40, 910-921.
23. Henzl, M. T., Agah, S. & Larson, J. D. (2003). Biochemistry, 42, 3594-3607.
24. Henzl, M. T., Agah, S. & Larson, J. D. (2004). Biochemistry, 43, 10906-10917.
25. Henzl, M. T. & Graham, J. S. (1999). FEBS Lett. 442, 241-245.
26. Henzl, M. T., Larson, J. D. & Agah, S. (2000). Biochemistry, 39, 5859-5867.
27. Henzl, M. T., Larson, J. D. & Agah, S. (2003). Anal. Biochem. 319, 216-233.
28. Henzl, M. T., Larson, J. D. & Agah, S. (2004). Biochemistry, 43, 2747-2763.
29. Henzl, M. T. & Tanner, J. J. (2008). Protein Sci. 17, 431-438.
30. Hubbard, S. J. & Thornton, J. M. (1993). NACCESS Computer Program, v.2.1.1. Department of Biochemistry and Molecular Biology, University College London, England.
31. Ikura, M. (1996). Trends Biochem. Sci. 21, 14-17.
32. Kauffman, J. F., Hapak, R. C. & Henzl, M. T. (1995). Biochemistry, 34, 991-1000.
33. Kissinger, C. R., Gehlhaar, D. K. & Fogel, D. B. (1999). Acta Cryst. D55, 484-491.
34. Kreiner, L. & Lee, A. (2006). J. Biol. Chem. 281, 4691-4698.
35. Kretsinger, J. K. & Schneider, J. P. (2003). J. Am. Chem. Soc. 125, 7907-7913.
36. Kretsinger, R. H. & Nockolds, C. E. (1973). J. Biol. Chem. 248, 3313-3326.
37. Kumar, S. & Nussinov, R. (1999). J. Mol. Biol. 293, 1241-1255.
38. Laskowski, R. A., Moss, D. S. & Thornton, J. M. (1993). J. Mol. Biol. 231, 1049-1067.
39. Levitt, M., Sander, C. & Stern, P. S. (1985). J. Mol. Biol. 181, 423-447.
40. Marqusee, S. & Sauer, R. T. (1994). Protein Sci. 3, 2217-2225.
41. Marti, D. N. & Bosshard, H. R. (2003). J. Mol. Biol. 330, 621-637.
42. McPhalen, C. A., Sielecki, A. R., Santarsiero, B. D. & James, M. N. (1994). J. Mol. Biol. 235, 718-732.
43. McPhalen, C. A., Strynadka, N. C. & James, M. N. (1991). Adv. Protein Chem. 42, 77-144.
44. Murphy, K. P. & Freire, E. (1992). Adv. Protein Chem. 43, 313-361.
45. Nakayama, S., Moncrief, N. D. & Kretsinger, R. H. (1992). J. Mol. Evol. 34, 416-448.
46. Palmisano, W. A., Trevino, C. L. & Henzl, M. T. (1990). J. Biol. Chem. 265, 14450-14456.
47. Permyakov, E. A., Medvedkin, V. N., Mitin, Y. V. & Kretsinger, R. H. (1991). Biochim. Biophys. Acta, 1076, 67-70.
48. Racay, P., Gregory, P. & Schwaller, B. (2006). FEBS J. 273, 96-108.
49. Reynolds, G. P., Abdul-Monim, Z., Neill, J. C. & Zhang, Z. J. (2004). Neurotox. Res. 6, 57-61.
50. Sakaguchi, N., Henzl, M. T., Thalmann, I., Thalmann, R. & Schulte, B. A. (1998). J. Histochem. Cytochem. 46, 29-40.
51. Sarakatsannis, J. N. & Duan, Y. (2005). Proteins, 60, 732-739.
52. Suhre, K. & Sanejouand, Y.-H. (2004a). Acta Cryst. D60, 796-799.
53. Suhre, K. & Sanejouand, Y.-H. (2004b). Nucleic Acids Res. 32, W610-W614.
54. Szatkowski, M. L., Westfall, M. V., Gomez, C. A., Wahr, P. A., Michele, D. E., DelloRusso, C., Turner, I. I., Hong, K. E., Albayya, F. P. & Metzger, J. M. (2001). J. Clin. Invest. 107, 191-198.
55. Thepaut, M., Strub, M.-P., Cavé, A., Baneères, J. L., Berchtold, M. W., Dumas, C. & Padilla, A. (2001). Proteins, 45, 117-128.
56. Wahr, P. A., Michele, D. E. & Metzger, J. M. (1999). Proc. Natl Acad. Sci. USA, 96, 11982-11985.
57. Wnuk, W., Cox, J. A. & Stein, E. A. (1982). Calcium and Cell Function, edited by W. Y. Cheung, pp. 243-278. New York: Academic Press.
58. Wouterlood, F. G., Vinkenoog, M. & van den Oever, M. (2002). Network, 13, 327-342.
59. Wu, Z., Li, X., de Leeuw, E., Ericksen, B. & Lu, W. (2005). J. Biol. Chem. 280, 43039-43047.
60. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. New York: John Wiley & Sons.
61. Xie, D. & Freire, E. (1994). J. Mol. Biol. 242, 62-80.
62. Yano, J. K. & Poulos, T. L. (2003). Curr. Opin. Biotechnol. 14, 360-365.
63. Yap, K. L., Ames, J. B., Swindells, M. B. & Ikura, M. (1999). Proteins, 37, 499-507.
64. Zhou, J. & Xu, Z. (2003). Nature Struct. Biol. 10, 942-947.