Structural insights into membrane targeting by the flagellar calcium-binding protein (FCaBP), a myristoylated and palmitoylated calcium sensor in Trypanosoma cruzi

Journal of Biological Chemistry

Volumn 283, Issue 34, 2008, Pages 23388-23396

  Wingard, Jennifer N ^a,e   Ladner, Jane ^a   Vanarotti, Murugendra ^b   Fisher, Andrew J ^b   Robinson, Howard ^c   Buchanan, Kathryn T ^d   Engman, David M ^d   Ames, James B ^a,b  

^a NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c BROOKHAVEN NATIONAL LABORATORY   (United States)

^d NORTHWESTERN UNIVERSITY   (United States)

^e UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ALLOYS; CRYSTAL STRUCTURE; MEMBRANES; NUCLEAR MAGNETIC RESONANCE; PORT TERMINALS; PROTEIN FOLDING; SOLVENTS;

ACYL GROUPS; BINDING PROTEINS; BOUND PROTEINS; BOUND STATES; CALCIUM SENSORS; CONFORMATIONAL CHANGES; FREE STATES; MYRISTOYLATION; N TERMINUSES; NMR ANALYSES; POSITIVE CHARGES; PROTEIN STRUCTURES; PROTEIN SURFACES; RECOVERIN; STRUCTURAL INSIGHTS; TERMINAL HELIXES; TERMINAL REGIONS; TRYPANOSOMA CRUZI; X-RAY CRYSTAL STRUCTURES;

CALCIUM;

CALCIUM; CALCIUM BINDING PROTEIN; GRANCALCIN; LYSINE; MONOMER; RECOVERIN; UNCLASSIFIED DRUG; FLAGELLAR CALCIUM BINDING PROTEIN, TRYPANOSOMA CRUZI; FLAGELLAR CALCIUM-BINDING PROTEIN, TRYPANOSOMA CRUZI; MYRISTIC ACID DERIVATIVE; PALMITIC ACID; PROTOZOAL PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; COVALENT BOND; CRYSTAL STRUCTURE; FLAGELLUM; MYRISTYLATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PALMITOYLATION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; TRYPANOSOMA CRUZI; AMINO ACID SEQUENCE; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; CONFORMATION; DIMERIZATION; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

PROTOZOA; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM-BINDING PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FLAGELLA; LYSINE; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MYRISTIC ACIDS; PALMITIC ACID; PROTEIN STRUCTURE, SECONDARY; PROTOZOAN PROTEINS; TRYPANOSOMA CRUZI;

EID: 53149089456     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M803178200     Document Type: Article

References (59)

1. Engman, D. M., Krause, K. H., Blumin, J. H., Kim, K. S., Kirchhoff, L. V., and Donelson, J. E. (1989) J. Biol. Chem. 264, 18627-18631
2. Moncrief, N. D., Kretsinger, R. H., and Goodman, M. (1990) J. Mol. Evol. 30, 522-562
3. Ikura, M. (1996) Trends Biochem. Sci. 21, 14-17
4. Buchanan, K. T., Ames, J. B., Asfaw, S. H., Wingard, J. N., Olson, C. L., Campana, P. T., Araujo, A. P., and Engman, D. M. (2005) J. Biol. Chem. 280, 40104-40111
5. Godsel, L. M., and Engman, D. M. (1999) EMBO J. 18, 2057-2065
6. Zozulya, S., and Stryer, L. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11569-11573
7. Dizhoor, A. M., Chen, C. K., Olshevskaya, E., Sinelnikova, V. V., Phillipov, P., and Hurley, J. B. (1993) Science 259, 829-832
8. Burgoyne, R. D. (2004) Biochim. Biophys. Acta 1742, 59-68
9. Ames, J. B., Ishima, R., Tanaka, T., Gordon, J. I., Stryer, L., and Ikura, M. (1997) Nature 389, 198-202
10. Kawamura, S. (1993) Nature 362, 855-857
11. Klenchin, V. A., Calvert, P. D., and Bownds, M. D. (1995) J. Biol. Chem. 270, 16147-16152
12. Erickson, M. A., Lagnado, L., Zozulya, S., Neubert, T. A., Stryer, L., and Baylor, D. A. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 6474-6479
13. Gray-Keller, M. P., Polans, A. S., Palczewski, K., and Detwiler, P. B. (1993) Neuron 10, 523-531
14. Koch, K. W., and Stryer, L. (1988) Nature 334, 64-66
15. Ridgley, E., Webster, P., Patton, C., and Ruben, L. (2000) Mol. Biochem. Parasitol. 109, 195-201
16. Tetley, L. (1986) Acta Trop. 43, 307-317
17. Tanaka, T., Ames, J. B., Harvey, T. S., Stryer, L., and Ikura, M. (1995) Nature 376, 444-447
18. Stephen, R., Bereta, G., Golczak, M., Palczewski, K., and Sousa, M. C. (2007) Structure 15, 1392-1402
19. Muchmore, D. C., McIntosh, L. P., Russell, C. B., Anderson, D. E., and Dahlquist, F. W. (1989) Methods Enzymol. 177, 44-86
20. McIntosh, L. P., and Dahlquist, F. W. (1990) Q. Rev. Biophys. 23, 1-38
21. Ames, J. B., Tanaka, T., Stryer, L., and Ikura, M. (1994) Biochemistry 33, 10743-10753
22. Jancarik, J., and Kim, S. H. (1991) J. Appl. Crystallogr. 24, 409-411
23. Pflugrath, J. W. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 1718-1725
24. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
25. Schneider, T. R., and Sheldrick, G. M. (2002) Acta Crystallogr. Sect. D Biol. Crystallogr.58, 1772-1779
26. Sheldrick, G. M. (2002) Kristallogr. 217, 644-650
27. Terwilliger, T. C. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 38-44
28. Terwilliger, T. C. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 45-49
29. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. Sect. D Biol. Crystallogr. 60, 2126-2132
30. Murshudov, D. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 140-255
31. Ames, J. B., Tanaka, T., Ikura, M., and Stryer, L. (1995) J. Biol. Chem. 270, 30909-30913
32. Lee, W., Revington, M. J., Arrowsmith, C., and Kay, L. E. (1994) FEBS Lett. 350, 87-90
33. Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., and Kay, L. E. (1994) Biochemistry 33, 5984-6003
34. Tanaka, T., Ames, J. B., Kainosho, M., Stryer, L., and Ikura, M. (1998) J. Biomol. NMR 11, 135-152
35. Deleted in proof
36. Deleted in proof
37. Jia, J., Han, Q., Borregaard, N., Lollike, K., and Cygler, M. (2000) J. Mol. Biol. 300, 1271-1281
38. Blanchard, H., Grochulski, P., Li, Y., Arthur, J. S., Davies, P. L., Elce, J. S., and Cygler, M. (1997) Nat. Struct. Mol. Biol. 4, 532-538
39. Schumacher, M. A., Crum, M., and Miller, M. C. (2004) Structure 12, 849-860
40. Zhang, M., Tanaka, T., and Ikura, M. (1995) Nat. Struct. Biol. 2, 758-767
41. Gagne, S. M., Tsuda, S., Li, M. X., Smillie, L. B., and Sykes, B. D. (1995) Nat. Struct. Biol. 2, 784-789
42. Hoeflich, K. P., and Ikura, M. (2002) Cell 108, 739-742
43. Vetter, S. W., and Leclerc, E. (2003) Eur. J. Biochem. 270, 404-414
44. Valentine, K., Mesleh, M., Ikura, M., Ames, J. B., and Opella, S. (2003) Biochemistry 42, 6333-6340
45. McLaughlin, S., and Aderem, A. (1995) Trends Biochem. Sci. 20, 272-276
46. Resh, M. D. (1994) Cell 76, 411-413
47. Flaherty, K. M., Zozulya, S., Stryer, L., and McKay, D. B. (1993) Cell 75, 709-716
48. Bourne, Y., Dannenberg, J., Pollmann, V. V., Marchot, P., and Pongs, O. (2001) J. Biol. Chem. 276, 11949-11955
49. Vijay-Kumar, S., and Kumar, V. D. (1999) Nat. Struct. Biol. 6, 80-88
50. Maki, M., Kitaura, Y., Satoh, H., Ohkouchi, S., and Shibata, H. (2002) Biochim. Biophys. Acta 1600, 51-60
51. Teahan, C. G., Totty, N. F., and Segal, A. W. (1992) Biochem. J. 286, 549-554
52. Meyers, M. B., Zamparelli, C., Verzili, D., Dicker, A. P., Blanck, T. J., and Chiancone, E. (1995) FEBS Lett. 357, 230-234
53. Mellgren, R. L. (1987) FASEB J. 1, 110-115
54. Lollike, K., Johnsen, A. H., Durussel, I., Borregaard, N., and Cox, J. A. (2001) J. Biol. Chem. 276, 17762-17769
55. Brownawell, A. M., and Creutz, C. E. (1997) J. Biol. Chem. 272, 22182-22190
56. Huttenlocher, A., Palecek, S. P., Lu, Q., Zhang, W., Mellgren, R. L., Lauffenburger, D. A., Ginsberg, M. H., and Horwitz, A. F. (1997) J. Biol. Chem. 272, 32719-32722
57. Maki, M., Narayana, S. V., and Hitomi, K. (1997) Biochem. J. 328, 718-720
58. Burgoyne, R. D., and Weiss, J. L. (2001) Biochem. J. 353, 1-12
59. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) Biochemistry 31, 1647-1651