Molecular recognition of chymotrypsin by the serine protease inhibitor ecotin from Yersinia pestis

Journal of Biological Chemistry

Volumn 286, Issue 27, 2011, Pages 24015-24022

  Clark, Elizabeth A ^a   Walker, Nicola ^b   Ford, Donna C ^b   Cooper, Ian A ^b   Oyston, Petra C F ^b   Acharya, K Ravi ^a  

^a University of Bath   (United Kingdom)

^b DEFENCE SCIENCE AND TECHNOLOGY LABORATORY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL THERAPY; BIODEFENSE; BIOTHREAT PATHOGENS; CAUSATIVE AGENTS; HUMAN PATHOGENS; MUTATIONAL ANALYSIS; RESISTANCE TO ANTIBIOTICS; SERINE PROTEASE INHIBITOR; STRUCTURE FEATURES; TETRAMERS; THERAPEUTIC USE; Y. PESTIS; YERSINIA PESTIS; YERSINIA PSEUDOTUBERCULOSIS;

AMINO ACIDS; BIOINFORMATICS; DIMERS; GENES; HEALTH CARE; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION;

PATHOGENS;

CHYMOTRYPSIN; DIMER; ECOTIN; SERINE PROTEINASE INHIBITOR; TETRAMER; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; ECOTIN GENE; ENZYME SPECIFICITY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; YERSINIA PESTIS;

CHYMOTRYPSIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; PERIPLASMIC PROTEINS; PLAGUE; PROTEIN STRUCTURE, QUATERNARY; SERINE PROTEINASE INHIBITORS; VIRULENCE FACTORS; YERSINIA PESTIS; YERSINIA PSEUDOTUBERCULOSIS;

BACTERIA (MICROORGANISMS); YERSINIA PESTIS; YERSINIA PSEUDOTUBERCULOSIS;

EID: 79959870539     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.225730     Document Type: Article

References (34)

1. Kohanski, M. A., Dwyer, D. J., and Collins, J. J. (2010) Nat. Rev. Microbiol. 8, 423-435
2. Achtman, M., Zurth, K., Morelli, G., Torrea, G., Guiyoule, A., and Carniel, E. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 14043-14048
3. Guiyoule, A., Gerbaud, G., Buchrieser, C., Galimand, M., Rahalison, L., Chanteau, S., Courvalin, P., and Carniel, E. (2001) Emerg. Infect. Dis. 7, 43-48
4. Hinnebusch, B. J., Rosso, M. L., Schwan, T. G., and Carniel, E. (2002) Mol. Microbiol. 46, 349-354
5. Parkhill, J., Wren, B. W., Thomson, N. R., Titball, R. W., Holden, M. T., Prentice, M. B., Sebaihia, M., James, K. D., Churcher, C., Mungall, K. L., Baker, S., Basham, D., Bentley, S. D., Brooks, K., Cerdeño-Tárraga, A. M., Chillingworth, T., Cronin, A., Davies, R. M., Davis, P., Dougan, G., Feltwell, T., Hamlin, N., Holroyd, S., Jagels, K., Karlyshev, A. V., Leather, S., Moule, S., Oyston, P. C., Quail, M., Rutherford, K., Simmonds, M., Skelton, J., Stevens, K., Whitehead, S., and Barrell, B. G. (2001) Nature 413, 523-527
6. Stubben, C. J., Duffield, M. L., Cooper, I. A., Ford, D. C., Gans, J. D., Karlyshev, A. V., Lingard, B., Oyston, P. C., de Rochefort, A., Song, J., Wren, B. W., Titball, R. W., and Wolinsky, M. (2009) BMC Genomics 10, 501
7. Chung, C. H., Ives, H. E., Almeda, S., and Goldberg, A. L. (1983) J. Biol. Chem. 258, 11032-11038
8. Derbise, A., Lesic, B., Dacheux, D., Ghigo, J. M., and Carniel, E. (2003) FEMS Immunol. Med. Microbiol. 38, 113-116
9. Maxson, M. E., and Darwin, A. J. (2004) J. Bacteriol. 186, 4199-4208
10. Riley, G., and Toma, S. (1989) J. Clin. Microbiol. 27, 213-214
11. Freter, R., Allweiss, B., O'Brien, P. C., Halstead, S. A., and Macsai, M. S. (1981) Infect. Immun. 34, 241-249
12. Taylor, R. K., Miller, V. L., Furlong, D. B., and Mekalanos, J. J. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 2833-2837
13. Wirnt, R. (1974) Methods of Enzymatic Analysis, 2nd Ed., Academic Press Inc., New York
14. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-325
15. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., and Read, R. J. (2007) J. Appl. Crystallogr. 40, 658-674
16. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Acta Crystallogr. D 66, 486-501
17. CCP4 (1994) Acta Crystallogr. D 50, 760-763
18. Brünger, A. T. (1992) Nature 355, 472-475
19. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
20. Lawrence, M. C., and Colman, P. M. (1993) J. Mol. Biol. 234, 946-950
21. Krissinel, E., and Henrick, K. (2007) J. Mol. Biol. 372, 774-797
22. Schechter, I., and Berger, A. (1967) Biochem. Biophys. Res. Commun. 27, 157-162
23. Eggers, C. T., Murray, I. A., Delmar, V. A., Day, A. G., and Craik, C. S. (2004) Biochem. J. 379, 107-118
24. Laws, T. R., Davey, M. S., Titball, R. W., and Lukaszewski, R. (2010) Microbes Infect. 12, 331-335
25. Seymour, J. L., Lindquist, R. N., Dennis, M. S., Moffat, B., Yansura, D., Reilly, D., Wessinger, M. E., and Lazarus, R. A. (1994) Biochemistry 33, 3949-3958
26. Ulmer, J. S., Lindquist, R. N., Dennis, M. S., and Lazarus, R. A. (1995) FEBS Lett. 365, 159-163
27. McGrath, M. E., Erpel, T., Bystroff, C., and Fletterick, R. J. (1994) EMBO J. 13, 1502-1507
28. Gillmor, S. A., Takeuchi, T., Yang, S. Q., Craik, C. S., and Fletterick, R. J. (2000) J. Mol. Biol. 299, 993-1003
29. Wang, S. X., Esmon, C. T., and Fletterick, R. J. (2001) Biochemistry 40, 10038-10046
30. Stoop, A. A., and Craik, C. S. (2003) Nat. Biotechnol. 21, 1063-1068
31. Perona, J. J., Tsu, C. A., Craik, C. S., and Fletterick, R. J. (1997) Biochemistry 36, 5381-5392
32. Bode, W., and Huber, R. (1992) Eur. J. Biochem. 204, 433-451
33. McDonald, I. K., and Thornton, J. M. (1994) J. Mol. Biol. 238, 777-793
34. Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., Lopez, R., Thompson, J. D., Gibson, T. J., and Higgins, D. G. (2007) Bioinformatics 23, 2947-2948