The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal β-barrel domain

Journal of Biological Chemistry

Volumn 279, Issue 45, 2004, Pages 47344-47351

  Nonaka, Tsuyoshi ^a   Fugihashi, Masahiro ^a   Kita, Akiko ^a   Saeki, Katsuhisa ^b   Ito, Susumu ^c   Horikoshi, Koki ^c   Miki, Kunio ^a,d  

^a KYOTO UNIVERSITY   (Japan)

^b KAO CORPORATION   (Japan)

^c JAPAN AGENCY FOR MARINE EARTH SCIENCE AND TECHNOLOGY   (Japan)

^d RIKEN Harima Institute/SPring 8 ^*  (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CATALYST ACTIVITY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; OXIDATION;

ANOMALOUS SCATTERING; BINDING ORIENTATION; TOPOLOGICAL ARCHITECTURES;

PROTEINS;

BETA CASEIN; CALCIUM ION; ENZYME KP 43; FURIN; KEXIN; SERINE PROTEINASE; SUBTILISIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BETA CHAIN; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPARATIVE STUDY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STABILITY; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; STRUCTURE ANALYSIS; TECHNIQUE;

ANIMALS; BACILLUS; BINDING SITES; CATALYSIS; CATTLE; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASE K; GENES, DOMINANT; GLYCINE; METHIONINE; MODELS, MOLECULAR; OXYGEN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERINE; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; SUBTILISINS; TIME FACTORS;

BACILLUS SP.;

EID: 8744220594     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M409089200     Document Type: Article

References (39)

1. Siezen, R. J., and Leunissen, J. A. (1997) Protein Sci. 6, 501-523
2. Wright, C. S., Alden, R. A., and Kraut, J. (1969) Nature 221, 235-242
3. Drenth, J., Hol, W. G., Jansonius, J. N., and Koekoek, R. (1972) Eur. J. Biochem. 26, 177-181
4. McPhalen, C. A., Schnebli, H. P., and James, M. N. (1985) FEBS Lett. 188, 55-58
5. Dauter, Z., Betzel, C., Hohne, W. E., Ingelman, M., and Wilson, K. S. (1988) FEBS Lett. 236, 171-178
6. Pahler, A., Banerjee, A., Dattagupta, J. K., Fujiwara, T., Lindner, K., Pal, G. P., Suck, D., Weber, G., and Saenger, W. (1984) EMBO J. 3, 1311-1314
7. Stauffer, C. E., and Etson, D. (1969) J. Biol. Chem. 244, 5333-5338
8. Bott, R., Ultsch, M., Kossiakoff, A., Graycar, T., Katz, B., and Power, S. (1988) J. Biol. Chem. 263, 7895-7906
9. Estell, D. A., Graycar, T. P., and Wells, J. A. (1985) J. Biol. Chem. 260, 6518-6521
10. Saeki, K., Hitomi, J., Okuda, M., Hatada, Y., Kageyama, Y., Takaiwa, M., Kubota, H., Hagihara, H., Kobayashi, T., Kawai, S., and Ito, S. (2002) Extremophiles 6, 65-72
11. Saeki, K., Okuda, M., Hatada, Y., Kobayashi, T., Ito, S., Takami, H., and Horikoshi, K. (2000) Biochem. Biophys. Res. Commun. 279, 313-319
12. Shaulsky, G., Kuspa, A., and Loomis, W. F. (1995) Genes Dev. 9, 1111-1122
13. Good, J. R., Cabrai, M., Sharma, S., Yang, J., Van Driessche, N., Shaw, C. A., Shaulsky, G., and Kuspa, A. (2003) Development 130, 2953-2965
14. Nonaka, T., Fujihashi, M., Kita, A., Saeki, K., Ito, S., and Miki, K. (2001) Acta Crystallogr. Sect. D Biol. Crystallogr. 57, 717-718
15. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
16. Rossmann, M. G., and van Beek, C. G. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 1631-1640
17. Collaborative Computational Project, Number 4 (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
18. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard (1991) Acta Crystallogr. A. 47, 110-119
19. 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. Sect. D Biol. Crystallogr. 54, 905-921
20. Sheldrick, G., and Schneider, T. (1997) Methods Enzymol. 277, 319-343
21. Anson, M. L. (1939) J. Gen. Physiol. 22, 79-89
22. Schagger, H., and von Jagow, G. (1987) Anal Biochem. 166, 368-379
23. Engh, R. A., and Huber, R. (1991) Acta Crystallogr. A. 47, 392-400
24. Ramachandran, G. N., and Sasisekharan, V. (1968) Adv. Protein Chem. 23, 283-438
25. Holyoak, T., Wilson, M. A., Fenn, T. D., Kettner, C. A., Petsko, G. A., Fuller, R. S., and Ringe, D. (2003) Biochemistry 42, 6709-6718
26. Henrich, S., Cameron, A., Bourenkov, G. P., Kiefersauer, R., Huber, R., Lindberg, I., Bode, W., and Than, M. E. (2003) Nat. Struct. Biol. 10, 520-526
27. Gluschankof, P., and Fuller, R. S. (1994) EMBO J. 13, 2280-2288
28. Zhou, A., Martin, S., Lipkind, G., LaMendola, J., and Steiner, D. F. (1998) J. Biol. Chem. 273, 11107-11114
29. Ueda, K., Lipkind, G. M., Zhou, A., Zhu, X., Kuznetsov, A., Philipson, L., Gardner, P., Zhang, C., and Steiner, D. F. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 5622-5627
30. Terada, I., Kwon, S. T., Miyata, Y., Matsuzawa, H., and Ohta, T. (1990) J. Biol. Chem. 265, 6576-6581
31. Kim, D. W., Lin, S. J., Morita, S., Terada, I., and Matsuzawa, H. (1997) Biochem. Biophys. Res. Commun. 231, 535-539
32. Kim, D. W., and Matsuzawa, H. (2000) Biochem. Biophys. Res. Commun. 277, 216-220
33. McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) Bioinformatics (Oxf.) 16, 404-405
34. Takeuchi, Y., Satow, Y., Nakamura, K. T., and Mitsui, Y. (1991) J. Mol. Biol. 221, 309-325
35. Schechter, I., and Berger, A. (1967) Biochem. Biophys. Res. Commun. 27, 157-162
36. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
37. Merritt, E. A., and Bacon, D. J. (1997) Methods Enzymol. 277, 505-524
38. Lawrence, M. C., and Bourke, P. (2000) J. Appl. Crystallogr. 33, 990-991
39. Nicholls, A., Sharp, K. A., and Honig, B. (1991) Proteins 11, 281-296