Differences in crystal and solution structures of the cytolethal distending toxin B subunit: Relevance to nuclear translocation and functional activation

Journal of Biological Chemistry

Volumn 281, Issue 35, 2006, Pages 25365-25372

  Hontz, Jill S ^a   Villar Lecumberri, Maria T ^a,b   Potter, Belinda M ^a   Yoder, Marilyn D ^a   Dreyfus, Lawrence A ^a   Laity, John H ^a  

^a UNIVERSITY OF MISSOURI KANSAS CITY   (United States)

^b UNIVERSITY OF KANSAS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELLS; CHEMICAL BONDS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DNA; ESCHERICHIA COLI; NUCLEAR MAGNETIC RESONANCE;

CELL CYCLE ARREST; CYTOLETHAL DISTENDING TOXIN (CDT); NUCLEAR TRANSLOCATION; SOLUTION STRUCTURES;

TOXIC MATERIALS;

ARGININE; CYTOLETHAL DISTENDING TOXIN; CYTOLETHAL DISTENDING TOXIN B; NITROGEN 15; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CELL CYCLE ARREST; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ESCHERICHIA COLI; INTOXICATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; TOXIN ANALYSIS; TOXIN STRUCTURE;

ACTIVE TRANSPORT, CELL NUCLEUS; ARGININE; BACTERIAL TOXINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

ESCHERICHIA COLI; EUKARYOTA;

EID: 33748744384     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M603727200     Document Type: Article

References (47)

1. Pickett, C. L., and Whitehouse, C. A. (1999) Trends Microbiol. 7, 292-297
2. Dreyfus, L. A. (2003) in Bacterial Protein Toxins (Burns, D., ed) pp. 257-270, ASM Press, Washington, D. C.
3. Lara-Tejero, M., and Galan, J. E. (2000) Science 290, 354-357
4. Elwell, C. A., and Dreyfus, L. A. (2000) Mol. Microbiol. 37, 952-963
5. de Rycke, J., and Oswald, E. (2001) FEMS Microbiol. Lett. 203, 141-148
6. Lara-Tejero, M., and Galan, J. E. (2001) Infect. Immun. 69, 4358-4365
7. Elwell, C., Chao, K. L., Patel, K., and Dreyfus, L. (2001) Infect. Immun. 69, 3418-3422
8. Cortes-Bratti, X., Chaves-Olarte, E., Lagergard, T., and Thelestam, M. (2000) Infect. Immun. 68, 6903-6911
9. Guerra, L., Teter, K., Lilley, B. N., Stenerlow, B., Holmes, R. K., Ploegh, H. L., Sandvig, K., Thelestam, M., and Frisan, T. (2005) Cell. Microbiol. 7, 921-934
10. Nesic, D., Hsu, Y., and Stebbins, C. E. (2004) Nature 429, 429-433
11. Yamada, T., Komoto, J., Saiki, K., Konishi, K., and Takusagawa, F. (2006) Protein Sci. 15, 362-372
12. McSweeney, L. A., and Dreyfus, L. A. (2004) Cell. Microbiol. 6, 447-458
13. Pickett, C. L., Cottle, D. L., Pesci, E. C., and Bikah, G. (1994) Infect. Immun. 62, 1046-1051
14. Aragon, V., Chao, K., and Dreyfus, L. A. (1997) Infect. Immun. 65, 3774-3780
15. Hontz, J. H., Villar-Lecumberri, M. T., Dreyfus, L. A., and Yoder, M. D. (2006). Acta Crystallogr. F62, 192-195
16. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
17. Navazza, J. (1994) Acta Crystallogr. Sect. A 50, 157-163
18. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sect. A 47, 110-119
19. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
20. Lamzin, V. S., Perrakis, A., and Wilson, K. S. (2001) in Crystallography of Biological Macromolecules (Rossman, M. G., and Arnold, E., eds) pp. 720-722, Kluwer Academic Publishers, Dordrecht, The Netherlands
21. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 240-255
22. Collaborative Computer Project Number 4 (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
23. Kabsch, W., and Sander, C. (1983) Biopolymers 22, 2577-2637
24. Guex, N., and Peitsch, M. C. (2006) Protein Data Bank Quarterly Newsletter 77, 7
25. Villar-Lecumberri, M. T., Potter, B. M., Wang, Z., Dreyfus, L., and Laity, J. H. (2006) J. Biomol. NMR 2006, 34
26. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) J. Mol. Biol. 222, 311-333
27. Braun, D., Wider, G., and Wuthrich, K. (1994) J. Am. Chem. Soc. 116, 8466-8469
28. Potter, B. M., Feng, L. S., Parasuram, P., Matskevich, V. A., Wilson, J. A., Andrews, G. K., and Laity, J. H. (2005) J. Biol. Chem. 280, 28529-28540
29. Palmer, A. G., III, Cavanagh, J., Wright, P. E., and Rance, M. (1991) J. Magn. Reson. 93, 151-170
30. Stone, M. J., Fairbrother, W. J., Palmer, A. G., III, Reizer, J., Saier, M. H., Jr., and Wright, P. E. (1992) Biochemistry 31, 4394-4406
31. Farrow, N. A., Zhang, O., Forman-Kay, J. D., and Kay, L. E. (1995) Biochemistry 34, 868-878
32. Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12594
33. Mandel, A. M., Akke, M., and Palmer, A. G., III (1995) J. Mol. Biol. 246, 144-163
34. Lipari, G., and Szabo, A. (1984) J. Am. Chem. Soc. 104, 4546-4549
35. Lipari, G., and Szabo, A. (1984) J. Am. Chem. Soc. 104, 4559-4570
36. Dosset, P., Hus, J. C., Blackledge, M., and Marion, D. (2000) J. Biomol. NMR 16, 23-28
37. Suck, D., Lahm, A., and Oefner, C. (1988) Nature 332, 464-468
38. Weston, S. A., Lahm, A., and Suck, D. (1992) J. Mol. Biol. 226, 1237-1256
39. Jones, S. J., Worrall, A. F., and Connolly, B. A. (1996) J. Mol. Biol. 264, 1154-1163
40. Dingwall, C., and Laskey, R. A. (1991) Trends Biochem. Sci. 16, 478-481
41. Palmer, A. G., III (2004) Chem. Rev. 104, 3623-3640
42. Cornilescu, G., Delaglio, F., and Bax, A. (1999) J. Biomol. NMR 13, 289-302
43. Conti, E., Uy, M., Leighton, L., Blobel, G., and Kuriyan, J. (1998) Cell 94, 193-204
44. Conti, E., and Kuriyan, J. (2000) Structure (Lond.) 8, 329-338
45. Fontes, M. R., Teh, T., and Kobe, B. (2000) J. Mol. Biol. 297, 1183-1194
46. Fontes, M. R., Teh, T., Toth, G., John, A., Pavo, I., Jans, D. A., and Kobe, B. (2003) Biochem. J. 375, 339-349
47. Nishikubo, S., Ohara, M., Ueno, Y., Ikura, M., Kurihara, H., Komatsuzawa, H., Oswald, E., and Sugai, M. (2003) J. Biol. Chem. 278, 50671-50681