High-resolution crystal structure of M-protease: Phylogeny aided analysis of the high-alkaline adaptation mechanism

Protein Engineering

Volumn 10, Issue 6, 1997, Pages 627-634

  Shirai, Tsuyoshi ^a   Suzuki, Atsuo ^a   Yamane, Takashi ^a   Ashida, Tamaichi ^a   Kobayashi, Tohru ^b   Hitomi, Jun ^b   Ito, Susumu ^b  

^a NAGOYA UNIVERSITY   (Japan)

^b KAO CORPORATION   (Japan)

Author keywords

Alkaline adaptation; Molecular phylogeny; Protein evolution; Subtilisin; X ray crystallography

Indexed keywords

ASPARAGINASE; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; SERINE PROTEINASE; SUBTILISIN;

ADAPTATION; ALKALINITY; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; ISOELECTRIC POINT; PHYLOGENY; PRIORITY JOURNAL;

BACILLUS SP.;

EID: 0030840103     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/10.6.627     Document Type: Article

References (38)

1. Adachi, J. and Hasegawa, M. (1992) Computer Science Monographs, No. 27, Molphy: Programs for Molecular Phylogenetics, I. - PROTML: Maximum Likelihood Inference of Protein Phylogeny. Institute of Statistical Mathematics, Tokyo.
2. Altschuh, D., Lesk, A.M., Bloomer, A.C. and Klug, A. (1987) J. Mol. Biol., 193, 693-707.
3. Betzel, C., Klupsch, S., Papendorf, G., Hastrup, S., Branner, S. and Wilson, K.S. (1992) J. Mol. Biol., 223, 427-445.
4. Brünger, A.T., Kuriyan, J. and Karplus, M. (1987) Science, 235, 458-460.
5. Cambillau, C. (1992) Turbo-FRODO, Molecular Graphics Program for Silicon Graphics IRIS 4D Series, Version 3.0. Bio-Graphics, Marseille, France.
6. Chu, N.-M., Chao, Y. and Bi, R.-C. (1995) Protein Engng, 8, 211-215.
7. Crowther, R.A. (1972) In Rossmann, M.G. (ed.), International Science Review, vol. 13, The Molecular Replacement Method. Gordon & Breach, New York, pp. 173-178.
8. Dauter, Z., Betzel, C, Höhne, W.-E., Ingelman, M. and Wilson, K.S. (1988) FEBS Lett., 236, 171-178.
9. Dayhoff, M.O., Schwartz, R.M. and Orcutt, B.C. (1978) In Dayhoff, M.O. (ed.), Atlas of Protein Sequence and Structure, vol. 5, supp. 3, National Biomedical Research Foundation, Washington DC, pp. 345-352.
10. Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D. and Klibanov, A.M. (1993) Proc. Natl Acad. Sci. USA, 90, 8653-8657.
11. Goddette, D.W., Paech, C., Yang, S.S., Mielenz, J.R., Bystroff, C., Wilke, M.E. and Fletterick, R.J. (1992) J. Mol. Biol., 228, 580-595.
12. Hakamada, Y., Kobayashi, T., Hitomi, J., Kawai, S. and Ito, S. (1994) J. Ferment. Bioengng, 78, 105-108.
13. Higashi, T. (1989) J. Appl. Crystallogr., 22, 9-18.
14. Jacobs, M., Eliasson, M., Uhlén, M. and Flock, J.-I. (1985) Nucleic Acids Res., 13, 8913-8926.
15. Jaenicke, R. (1991) Eur. J. Biochem., 202, 715-728.
16. Jang, J.S., Kang, D.O., Chun, M.J. and Byun, S.M. (1992) Biochem. Biophys. Res. Commun., 184, 277-282.
17. Kaneko, R., Koyama, N., Tsai, Y.-C., Juang, R.-Y., Yoda, K. and Yamasaki, M. (1989) J. Bacteriol., 171, 5232-5236.
18. Kishino, H., Miyata, T. and Hasegawa, M. (1990) J. Mol. Evol., 31, 151-160.
19. Kobayashi, T., Hakamada, Y., Adachi, S., Hitomi, J., Yoshimatsu, T., Koike, K., Kawai, S. and Ito, S. (1995) Appl. Microbiol. Biothechnol., 43, 473-481.
20. Kraut, J. (1977) Annu. Rev. Biochem., 46, 331-358.
21. Van Der Laan, J.C., Gerritse, G., Mulleners, L.J.S.M., Van Der Hoek, R.A.C. and Quax, W.J. (1991) Appl. Environ. Microbiol., 57, 901-909.
22. Van Der Laan, J.M., Teplyakov, A.V., Kelders, H., Kalk, K.H., Misset, O., Mulleners, L.J.S.M. and Dijkstra, B.W. (1992) Protein Engng, 5, 405-411.
23. Luzzati, P.V. (1952) Acta Crystallogr., 5, 802-810.
24. Markland, F.S. and Smith, E.L. (1967) J. Biol. Chem., 242, 5198-5211.
25. Markland, F.S. and Smith, E.L. (1971) In Boyer, P.D. (ed.), The Enzymes. Academic Press, New York, vol.3, pp. 561-608.
26. Matsubara, H., Hagihara, B., Nakai, M., Komaki, T., Yonetani, T. and Okunuki, K. (1958) J. Biochem., 45, 251-258.
27. McPhalen, C.A., Schnebli, H.P. and James, M.N.G. (1985) FEBS Lett., 188, 55-58.
28. Pähler, 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.
29. Saitou, N. and Nei, M. (1987) Mol. Biol. Evol., 4, 406-425.
30. Sakabe, N. (1983) J. Appl. Crystallogr., 16, 542-547.
31. Shindyalov, I.N., Kolchanov, N.A. and Sander, C. (1994) Protein Engng, 7, 349-358.
32. Sloma, A., Rufo, G.A., Rudolph, C.F., Sullivan, B.J., Theriault, K.A. and Pero, J. (1990) J. Bacteriol., 172, 1470-1477.
33. Sobek, H., Hecht, H.J., Hofmann, B., Aehle, W. and Schomburg, D. (1990) FEBS Lett., 274, 57-60.
34. Stewart, C.-B., Schilling, J.W. and Wilson, A.C. (1987) Nature, 330, 401-404.
35. Tsai, Y.-C., Lin, S.-F., Li, Y.-F., Yamasaki, M. and Tamura, G. (1986) Biochim. Biophys. Acta. 883, 439-447.
36. Wright, C.S., Alden, R.A. and Kraut, J. (1969) Nature, 221, 235-242.
37. Wu, X.-C., Nathoo, S., Pang, A.S.-H., Carne, T. and Wong, S.-L. (1990) J. Biol. Chem., 265, 6845-6850.
38. Yamane, T., Kani, T., Hatanaka, T., Suzuki, A., Ashida, T., Kobayashi, T., Ito, S. and Yamashita, O. (1995) Acta Crystallogr., D51, 199-206.