Structural insights into inhibition of Bacillus anthracis sporulation by a novel class of non-heme globin sensor domains

Journal of Biological Chemistry

Volumn 286, Issue 10, 2011, Pages 8448-8458

  Stranzl, Gudrun R ^a   Santelli, Eugenio ^a   Bankston, Laurie A ^a   La Clair, Chandra ^b   Bobkov, Andrey ^a   Schwarzenbacher, Robert ^a,d   Godzik, Adam ^a   Perego, Marta ^b   Grynberg, Marcin ^a,c   Liddington, Robert C ^a  

^a BURNHAM INSTITUTE   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^d UNIVERSITY OF SALZBURG   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRACIS; BACILLUS ANTHRACIS; BACTERIAL GENOMES; CHLORIDE ION CONCENTRATION; CHLORIDE IONS; ENCODED PROTEINS; ENVIRONMENTAL CUES; ENVIRONMENTAL SIGNALS; FATTY ACID SYNTHESIS; HEAD GROUPS; HISTIDINE KINASE; HYDROPHOBIC TUNNEL; IMMUNE SURVEILLANCE; IN-VIVO; OVER-EXPRESSION; PLASMID PROTEINS; SENSOR DOMAINS; SEQUENCE IDENTITY; STRUCTURAL INSIGHTS; STRUCTURE-BASED; VEGETATIVE CELLS; VIRULENCE FACTORS; VIRULENCE GENE;

AMINO ACIDS; BACILLI; BACTERIOLOGY; CHLORINE COMPOUNDS; ENZYMES; FATTY ACIDS; GENE EXPRESSION; GENE EXPRESSION REGULATION; PORPHYRINS; SENSORS;

HEMOGLOBIN;

ARGININE; CHLORIDE ION; FATTY ACID; GLOBIN; PROTEIN ATXA; PROTEIN BA2291; PROTEIN HISTIDINE KINASE; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS ANTHRACIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; SPOROGENESIS; UPREGULATION;

BACILLUS ANTHRACIS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TRANS-ACTIVATORS; VIRULENCE FACTORS;

BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS);

EID: 79953150407     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.207126     Document Type: Article

References (45)

1. Okinaka, R. T., Cloud, K., Hampton, O., Hoffmaster, A. R., Hill, K. K., Keim, P., Koehler, T. M., Lamke, G., Kumano, S., Mahillon, J., Manter, D., Martinez, Y., Ricke, D., Svensson, R., and Jackson, P. J. (1999) J. Bacteriol. 181, 6509-6515
2. Ezzell, J. W., and Welkos, S. L. (1999) J. Appl. Microbiol. 87, 250
3. Candela, T., Mock, M., and Fouet, A. (2005) J. Bacteriol. 187, 7765-7772
4. Mock, M., and Fouet, A. (2001) Annu. Rev. Microbiol. 55, 647-671
5. Kang, T. J., Fenton, M. J., Weiner, M. A., Hibbs, S., Basu, S., Baillie, L., and Cross, A. S. (2005) Infect. Immun. 73, 7495-7501
6. Drysdale, M., Heninger, S., Hutt, J., Chen, Y., Lyons, C. R., and Koehler, T. M. (2005) EMBO J. 24, 221-227
7. Hu, H., Sa, Q., Koehler, T. M., Aronson, A. I., and Zhou, D. (2006) Cell. Microbiol. 8, 1634-1642
8. Perego, M., and Hoch, J. A. (2008) Trends Microbiol. 16, 215-221
9. Dai, Z., Sirard, J. C., Mock, M., and Koehler, T. M. (1995) Mol. Microbiol. 16, 1171-1181
10. Uchida, I., Hornung, J. M., Thorne, C. B., Klimpel, K. R., and Leppla, S. H. (1993) J. Bacteriol. 175, 5329-5338
11. Drysdale, M., Bourgogne, A., Hilsenbeck, S. G., and Koehler, T. M. (2004) J. Bacteriol. 186, 307-315
12. Bourgogne, A., Drysdale, M., Hilsenbeck, S. G., Peterson, S. N., and Koehler, T. M. (2003) Infect. Immun. 71, 2736-2743
13. Mignot, T., Mock, M., and Fouet, A. (2003) Mol. Microbiol. 47, 917-927
14. Hadjifrangiskou, M., Chen, Y., and Koehler, T. M. (2007) J. Bacteriol. 189, 1874-1883
15. Saile, E., and Koehler, T. M. (2002) J. Bacteriol. 184, 370-380
16. Stephenson, K., and Hoch, J. A. (2002) Mol. Microbiol. 46, 297-304
17. Brunsing, R. L., La Clair, C., Tang, S., Chiang, C., Hancock, L. E., Perego, M., and Hoch, J. A. (2005) J. Bacteriol. 187, 6972-6981
18. Bongiorni, C., Stoessel, R., Shoemaker, D., and Perego, M. (2006) J. Bacteriol. 188, 487-498
19. Bongiorni, C., Stoessel, R., and Perego, M. (2007) J. Bacteriol. 189, 2637-2645
20. Szurmant, H., and Hoch, J. A. (2010) Curr. Opin. Microbiol. 13, 190-197
21. Scaramozzino, F., White, A., Perego, M., and Hoch, J. A. (2009) J. Bacteriol. 191, 687-692
22. White, A. K., Hoch, J. A., Grynberg, M., Godzik, A., and Perego, M. (2006) J. Bacteriol. 188, 6354-6360
23. Harrison, C. J., Bohm, A. A., and Nelson, H. C. (1994) Science 263, 224-227
24. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
25. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. D Biol. Crystallogr. 55, 849-861
26. Terwilliger, T. C. (2001) Acta Crystallogr. D Biol Crystallogr. 57, 1755-1762
27. Kleywegt, G. J., Zou, J. Y., Kjeldgaard, M., and Jones, T. A. (2001) in International Tables for Crystallography: Crystallography of Biological Macromolecules (Rossmann, M. G., and Arnold, E., eds) pp. 353-356, Kluwer Academic Publishers, Dordrecht, The Netherlands
28. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
29. Brünger, 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. D Biol. Crystallogr. 54, 905-921
30. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
31. Biegert, A., and Söding, J. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 3770-3775
32. Holm, L., and Sander, C. (1993) J. Mol. Biol. 233, 123-138
33. Murray, J. W., Delumeau, O., and Lewis, R. J. (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 17320-17325
34. de Sanctis, D., Dewilde, S., Pesce, A., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., and Bolognesi, M. (2004) J. Mol. Biol. 336, 917-927
35. Contreras-Martel, C., Matamala, A., Bruna, C., Poo-Caamaño, G., Almonacid, D., Figueroa, M., Martínez-Oyanedel, J., and Bunster, M. (2007) Biophys. Chem. 125, 388-396
36. Zhang, W., and Phillips, G. N., Jr. (2003) Structure 11, 1097-1110
37. Song, Y., and Gunner, M. R. (2009) J. Mol. Biol. 387, 840-856
38. Gut, H., Pennacchietti, E., John, R. A., Bossa, F., Capitani, G., De Biase, D., and Grütter, M. G. (2006) EMBO J. 25, 2643-2651
39. Dhe-Paganon, S., Duda, K., Iwamoto, M., Chi, Y. I., and Shoelson, S. E. (2002) J. Biol. Chem. 277, 37973-37976
40. Nogi, Y., Takami, H., and Horikoshi, K. (2005) Int. J. Syst. Evol. Microbiol. 55, 2309-2315
41. Sakurai, H., Ogawa, T., Shiga, M., and Inoue, K. (2010) Photosynth. Res. 104, 163-176
42. Pérez-Pantoja, D., De la Iglesia, R., Pieper, D. H., and González, B. (2008) FEMS Microbiol. Rev. 32, 736-794
43. Aguilar, P. S., Hernandez-Arriaga, A. M., Cybulski, L. E., Erazo, A. C., and de Mendoza, D. (2001) EMBO J. 20, 1681-1691
44. Lodish, H., Baltimore, D., Berk, A., Zipursky, L. S., Matsudaira, P., and Darnell, J. (2000) Molecular Cell Biology, 4th Ed., pp. 640-641, W. H. Freeman and Company, New York
45. Giardina, B., Mosca, D., and De Rosa, M. C. (2004) Acta Physiol. Scand. 182, 229-244