Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 69, Issue 9, 2013, Pages 1052-1059

  Hadži, San ^a,b,c   Garcia Pino, Abel ^a,b   Martinez Rodriguez, Sergio ^a,b,d   Verschueren, Koen ^a,b   Christensen Dalsgaard, Mikkel ^e   Gerdes, Kenn ^e   Lah, Jurij ^c   Loris, Remy ^a,b  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c UNIVERSITY OF LJUBLJANA   (Slovenia)

^d UNIVERSITY OF ALMERÍA   (Spain)

^e NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

intrinsic disorder; macromolecular complexes; persistence; ribonucleases; toxin antitoxin modules

Indexed keywords

ANTITOXIN; CHOLERA TOXIN; RECOMBINANT PROTEIN; RIBONUCLEASE;

ARTICLE; CHEMISTRY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; INTRINSIC DISORDER; ISOLATION AND PURIFICATION; MACROMOLECULAR COMPLEXES; MASS SPECTROMETRY; PATHOGENICITY; PERSISTENCE; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; TOXIN-ANTITOXIN MODULES; VIBRIO CHOLERAE; X RAY CRYSTALLOGRAPHY;

INTRINSIC DISORDER; MACROMOLECULAR COMPLEXES; PERSISTENCE; RIBONUCLEASES; TOXIN-ANTITOXIN MODULES;

ANTITOXINS; CHOLERA TOXIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GENE EXPRESSION; MASS SPECTROMETRY; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; VIBRIO CHOLERAE;

EID: 84883428186     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309113021490     Document Type: Article

References (59)

1. Anantharaman, V. & Aravind, L. (2003). Genome Biol. 4, R81.
2. Arbing, M. A. et al. (2010). Structure, 18, 996-1010.
3. Bggild, A., Sofos, N., Andersen, K. R., Feddersen, A., Easter, A. D., Passmore, L. A. & Brodersen, D. E. (2012). Structure, 20, 1641-1648.
4. Brown, B. L., Grigoriu, S., Kim, Y., Arruda, J. M., Davenport, A., Wood, T. K., Peti, W. & Page, R. (2009). PLoS Pathog. 5, e1000706.
5. Budde, P. P., Davis, B. M., Yuan, J. & Waldor, M. K. (2007). J. Bacteriol. 189, 491-500.
6. Buts, L., Lah, J., Dao-Thi, M.-H., Wyns, L. & Loris, R. (2005). Trends Biochem. Sci. 30, 672-679.
7. Camacho, A. G., Misselwitz, R., Behlke, J., Ayora, S., Welfle, K., Meinhart, A., Lara, B., Saenger, W., Welfle, H. & Alonso, J. C. (2002). Biol. Chem. 383, 1701-1713.
8. Christensen-Dalsgaard, M. & Gerdes, K. (2006). Mol. Microbiol. 62, 397-411.
9. Christensen-Dalsgaard, M., Jrgensen, M. G. & Gerdes, K. (2010). Mol. Microbiol. 75, 333-348.
10. Dalton, K. M. & Crosson, S. (2010). Biochemistry, 49, 2205-2215.
11. David, G. & Pe rez, J. (2009). J. Appl. Cryst. 42, 892-900.
12. De Jonge, N., Garcia-Pino, A., Buts, L., Haesaerts, S., Charlier, D., Zangger, K., Wyns, L., De Greve, H. & Loris, R. (2009). Mol. Cell, 35, 154-163.
13. Drobnak, I., De Jonge, N., Haesaerts, S., Vesnaver, G., Loris, R. & Lah, J. (2013). J. Am. Chem. Soc. 135, 1288-1294.
14. Fischer, H., de Oliveira Neto, M., Napolitano, H. B., Polikarpov, I. & Craievich, A. F. (2010). J. Appl. Cryst. 43, 101-109.
15. Garcia-Pino, A., Balasubramanian, S., Wyns, L., Gazit, E., De Greve, H., Magnuson, R. D., Charlier, D., van Nuland, N. A. & Loris, R. (2010). Cell, 142, 101-111.
16. Garcia-Pino, A., Christensen-Dalsgaard, M., Wyns, L., Yarmolinsky, M., Magnuson, R. D., Gerdes, K. & Loris, R. (2008). J. Biol. Chem. 283, 30821-30827.
17. Gerdes, K., Christensen, S. K. & Lbner-Olesen, A. (2005). Nature Rev. Microbiol. 3, 371-382.
18. Gerdes, K., Rasmussen, P. B. &Molin, S. (1986). Proc. Natl Acad. Sci. USA, 83, 3116-3120.
19. Gill, S. C. & von Hippel, P. H. (1989). Anal. Biochem. 182, 319-326.
20. Gonza lez Barrios, A. F., Zuo, R., Hashimoto, Y., Yang, L., Bentley, W. E. & Wood, T. K. (2006). J. Bacteriol. 188, 305-316.
21. Guinier, A. (1939). Ann. Phys. 12, 161-237.
22. Heidelberg, J. F. et al. (2000). Nature (London), 406, 477-483.
23. Heinemann, U. & Saenger, W. (1982). Nature (London), 299, 27-31.
24. Hurley, J. M. & Woychik, N. A. (2009). J. Biol. Chem. 284, 18605-18613.
25. Jrgensen, M. G., Pandey, D. P., Jaskolska, M. & Gerdes, K. (2009). J. Bacteriol. 191, 1191-1199.
26. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
27. Kamada, K. & Hanaoka, F. (2005). Mol. Cell, 19, 497-509.
28. Kamada, K., Hanaoka, F. & Burley, S. K. (2003). Mol. Cell, 11, 875-884.
29. Kantardjieff, K. A. & Rupp, B. (2003). Protein Sci. 12, 1865-1871.
30. Kasari, V., Kurg, K., Margus, T., Tenson, T. & Kaldalu, N. (2010). J. Bacteriol. 192, 2908-2919.
31. Keren, I., Shah, D., Spoering, A., Kaldalu, N. & Lewis, K. (2004). J. Bacteriol. 186, 8172-8180.
32. Khoo, S. K., Loll, B., Chan, W. T., Shoeman, R. L., Ngoo, L., Yeo, C. C. &Meinhart, A. (2007). J. Biol. Chem. 282, 19606-19618.
33. Konarev, P. V., Petoukhov, M. V., Volkov, V. V. & Svergun, D. I. (2006). J. Appl. Cryst. 39, 277-286.
34. Lehnherr, H. & Yarmolinsky, M. B. (1995). Proc. Natl Acad. Sci. USA, 92, 3274-3277.
35. Leplae, R., Geeraerts, D., Hallez, R., Guglielmini, J., Dreze, P. & VanMelderen, L. (2011). Nucleic Acids Res. 39, 5513-5525.
36. Li, G.-Y., Zhang, Y., Inouye, M. & Ikura, M. (2008). J. Mol. Biol. 380, 107-119.
37. Li, G.-Y., Zhang, Y., Inouye, M. & Ikura, M. (2009). J. Biol. Chem. 284, 14628-14636.
38. Loris, R., Marianovsky, I., Lah, J., Laeremans, T., Engelberg-Kulka, H., Glaser, G., Muyldermans, S. & Wyns, L. (2003). J. Biol. Chem. 278, 28252-28257.
39. Madl, T., Van Melderen, L., Mine, N., Respondek, M., Oberer, M., Keller, W., Khatai, L. & Zangger, K. (2006). J. Mol. Biol. 364, 170-185.
40. Maisonneuve, E., Shakespeare, L. J., Jrgensen, M. G. & Gerdes, K. (2011). Proc. Natl Acad. Sci. USA, 108, 13206-13211.
41. Makarova, K. S., Wolf, Y. I. & Koonin, E. V. (2009). Biol. Direct, 4, 19
42. Mate, M. J., Vincentelli, R., Foos, N., Raoult, D., Cambillau, C. & Ortiz-Lombard?a, M. (2012). Nucleic Acids Res. 40, 3245-3258.
43. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
44. Mattison, K., Wilbur, J. S., So, M. & Brennan, R. G. (2006). J. Biol. Chem. 281, 37942-37951.
45. Mauguen, Y., Hartley, R. W., Dodson, E. J., Dodson, G. G., Bricogne, G., Chothia, C. & Jack, A. (1982). Nature (London), 297, 162-164.
46. Meinhart, A., Alonso, J. C., Stra ter, N. & Saenger, W. (2003). Proc. Natl Acad. Sci. USA, 100, 1661-1666.
47. Oberer, M., Zangger, K., Gruber, K. & Keller, W. (2007). Protein Sci. 16, 1676-1688.
48. Pandey, D. P. & Gerdes, K. (2005). Nucleic Acids Res. 33, 966-976.
49. Perez-Iratxeta, C. & Andrade-Navarro, M. A. (2008). BMC Struct. Biol. 8, 25.
50. Schumacher, M. A., Piro, K. M., Xu, W., Hansen, S., Lewis, K. & Brennan, R. G. (2009). Science, 323, 396-401.
51. Sevin, E. W. & Barloy-Hubler, F. (2007). Genome Biol. 8, R155.
52. Takagi, H., Kakuta, Y., Okada, T., Yao, M., Tanaka, I. & Kimura, M. (2005). Nature Struct. Mol. Biol. 12, 327-331.
53. Tian, Q. B., Ohnishi, M., Tabuchi, A. & Terawaki, Y. (1996). Biochem. Biophys. Res. Commun. 220, 280-284.
54. Tripathi, A., Dewan, P. C., Barua, B. & Varadarajan, R. (2012). Proc. NatlAcad. Sci. USA, 109, 12497-12502.
55. Van Melderen, L., Dao Thi, M. H., Lecchi, P., Gottesman, S., Couturier, M. &Maurizi, M. R. (1996). J. Biol. Chem. 271, 27730-27738.
56. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
57. Yamaguchi, Y., Park, J.-H. & Inouye, M. (2009). J. Biol. Chem. 284, 28746-28753.
58. Yamaguchi, Y., Park, J.-H. & Inouye, M. (2011). Annu. Rev. Genet. 45, 61-79.
59. Yang, X. & Moffat, K. (1996). Structure, 4, 837-852.