Driving forces of gyrase recognition by the addiction toxin CcdB

Journal of Biological Chemistry

Volumn 284, Issue 30, 2009, Pages 20002-20010

  Simic, Mario ^a   De Jonge, Natalie ^b   Loris, Remy ^b   Vesnaver, Gorazd ^a   Lah, Jurij ^a  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; BINDING ENERGETICS; CATALYTIC DOMAINS; DIMERIZATION DOMAIN; DRIVING FORCES; EXPERIMENTAL DATA; ISOTHERMAL TITRATION CALORIMETRY; MODEL ANALYSIS; PROCESS-DRIVEN; QUINOLONES; SPECIFIC INTERACTION; STRUCTURAL INFORMATION; STRUCTURAL REARRANGEMENT; THERMO DYNAMIC ANALYSIS; TOPOISOMERASE;

BACTERIOLOGY; BINDING ENERGY; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; ESCHERICHIA COLI; THERMOANALYSIS; TOXIC MATERIALS; UREA;

BINDING SITES;

BACTERIAL TOXIN; BACTERIAL TOXIN CCDB; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE (ATP HYDROLYSING) A; UNCLASSIFIED DRUG; UREA;

ARTICLE; CIRCULAR DICHROISM; ENTHALPY; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; ISOTHERMAL TITRATION CALORIMETRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; THERMODYNAMICS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BACTERIAL TOXINS; CALORIMETRY; CIRCULAR DICHROISM; DNA GYRASE; ESCHERICHIA COLI; F FACTOR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMODYNAMICS; TITRIMETRY; UREA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 67749110273     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.014035     Document Type: Article

References (44)

1. Nöllmann, M., Crisona, N. J., and Arimondo, P. B. (2007) Biochimie. 89, 490-499
2. Schoeffler, A. J., and Berger, J. M. (2005) Biochem. Soc. Trans. 33, 1465-1470
3. Reece, R. J., and Maxwell, A. (1991) Crit. Rev. Biochem. Mol. Biol. 26, 335-375
4. Maxwell, A. (1997) Trends Microbiol. 5, 102-109
5. Bernard, P., and Couturier, M. (1992) J. Mol. Biol. 226, 735-745
6. Miki, T., Park, J. A., Nagao, K., Murayama, N., and Horiuchi, T. (1992) J. Mol. Biol. 225, 39-52
7. Dao-Thi, M. H., Van Melderen, L., De Genst, E., Afif, H., Buts, L., Wyns, L., and Loris, R. (2005) J. Mol. Biol. 348, 1091-1102
8. Buts, L., Lah, J., Dao-Thi, M. H., Wyns, L., and Loris, R. (2005) Trends Biochem. Sci. 30, 672-679
9. Reece, R. J., and Maxwell, A. (1989) J. Biol. Chem. 264, 19648-19653
10. Morais Cabral, J. H., Jackson, A. P., Smith, C. V., Shikotra, N., Maxwell, A., and Liddington, R. C. (1997) Nature 388, 903-906
11. Bahassi, E. M., O'Dea, M. H., Allali, N., Messens, J., Gellert, M., and Couturier, M. (1999) J. Biol. Chem. 274, 10936-10944
12. Ladbury, J. E., and Chowdhry, B. Z. (1998) Biocalorimetry: Applications of Calorimetry in the Biological Sciences, John Wiley, Chichester, UK
13. Lopez, M. M., and Makhatadze, G. I. (2002) Methods Mol. Biol. 173, 121-126
14. Chaires, J. B. (1997) Biopolymers 44, 201-215
15. Loris, R., Marianovsky, I., Lah, J., Laeremans, T., Engelberg-Kulka, H., Glaser, G., Muyldermans, S., and Wyns, L. (2003) J. Biol. Chem. 278, 28252-28257
16. Lah, J., Marianovsky, I., Glaser, G., Engelberg-Kulka, H., Kinne, J., Wyns, L., and Loris, R. (2003) J. Biol. Chem. 278, 14101-14111
17. Lah, J., and Vesnaver, G. (2004) J. Mol. Biol. 342, 73-89
18. Dao-Thi, M. H., Charlier, D., Loris, R., Maes, D., Messens, J., Wyns, L., and Backmann, J. (2002) J. Biol. Chem. 277, 3733-3742
19. Buts, L., De Jonge, N., Loris, R., Wyns, L., and Dao-Thi, M. H. (2005) Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 61, 949-952
20. Dao-Thi, M. H., Van Melderen, L., De Genst, E., Buts, L., Ranquin, A., Wyns, L., and Loris, R. (2004) Acta Crystallogr. Biol. Crystallogr. 60, 1132-1134
21. Reece, R. J., and Maxwell, A. (1991) J. Biol. Chem. 266, 3540-3546
22. Gill, S. C., and von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326
23. Myers, J. K., Pace, C. N., and Scholtz, M. J. (1995) Protein Sci. 4, 2138-2148
24. Press, W. H., Flannery, B. P., Teukolsky, S. A., and Vetterling, W. T. (1992) Numerical Recipes, pp. 650-694, Cambridge University Press, Oxford, UK
25. Lah, J., Drobnak, I., Dolinar, M., and Vesnaver, G. (2008) Nucleic Acids Res. 36, 897-904
26. Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Anal. Biochem. 179, 131-137
27. Lah, N., Lah, J., Zegers, I., Wyns, L., and Messens, J. (2003) J. Biol. Chem. 278, 24673-24679
28. Murphy, K. P., and Freire, E. (1992) Adv. Protein Chem. 43, 313-361
29. Makhatadze, G. I., and Privalov, P. L. (1995) Adv. Protein Chem. 47, 307-425
30. Spolar, R. S., and Record, M. T., Jr. (1994) Science 263, 777-784
31. Robertson, A. D., and Murphy, K. P. (1997) Chem. Rev. 97, 1251-1268
32. Hubbard, S. J., and Thornton, J. M. (1993) NACCESS, University College, London
33. Loris, R., Dao-Thi, M. H., Bahassi, E. M., Van Melderen, L., Poortmans, F., Liddington, R., Couturier, M., and Wyns, L. (1999) J. Mol. Biol. 285, 1667-1677
34. Xie, D., and Freire, E. (1994) Proteins Struct. Funct. Genet. 19, 291-301
35. Lah, J., Simic, M., Vesnaver, G., Marianovsky, I., Glaser, G., Engelberg-Kulka, H., and Loris, R. (2005) J. Biol. Chem. 280, 17397-17407
36. Lah, J., Prislan, I., Krzan, B., Salobir, M., Francky, A., and Vesnaver, G. (2005) Biochemistry 44, 13883-13892
37. Lah, J., Bester-Rogac, M., Perger, T. M., and Vesnaver, G. (2006) J. Phys. Chem. B 110, 23279-26291
38. Lee, K. H., Xie, D., Freire, E., and Amzel, L. M. (1994) Proteins Struct. Funct. Genet. 20, 68-84
39. Baldwin, R. L. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 8069-8072
40. Baker, B. M., and Murphy, K. P. (1997) J. Mol. Biol. 268, 557-569
41. Dao-Thi, M. H., Messens, J., Wyns, L., and Backmann, J. (2000) J. Mol. Biol. 299, 1373-1386
42. Bajaj, K., Chakshusmathi, G., Bachhawat-Sikder, K., Surolia, A., and Varadarajan, R. (2004) Biochem. J. 380, 409-417
43. Bradshaw, J. M., and Waksman, G. (1998) Biochemistry 37, 15400-15407
44. Kampranis, S. C., Howells, A. J., and Maxwell, A. (1999) J. Mol. Biol. 293, 733-744