Two flexible loops in subtilisin-like thermophilic protease, thermicin, from Thermoanaerobacter yonseiensis

Journal of Biochemistry and Molecular Biology

Volumn 35, Issue 5, 2002, Pages 498-507

  Hyeung, Jin Jang ^a   Lee, Chang Hun ^a   Lee, Weontae ^a   Yu, Sam Kim ^a  

^a Yonsei University   (South Korea)

Author keywords

Thermicin; Thermoanaerobacter yonseiensis; Thermophilic protease

Indexed keywords

ESCHERICHIA COLI; THERMOANAEROBACTER YONSEIENSIS;

PROTEINASE;

AMINO ACID SEQUENCE; ANAEROBIC BACTERIUM; ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENE DELETION; GENETICS; HEAT; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BACTERIA, ANAEROBIC; CATALYSIS; ENDOPEPTIDASES; ENZYME STABILITY; HEAT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SEQUENCE DELETION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0037200990     PISSN: 12258687     EISSN: 12258687     Source Type: Journal    
DOI: None     Document Type: Article

References (39)

1. Argos, P., Rosseman, M. G., Gsau, U. M., Zuber, H., Frank, G. and Tratschin, J. D. (1979) Thermal stability and protein structure. Biochemistry 18, 5698-5703.
2. Bacon, D. J. and Anderson, W. F. (1988) A Fast Algorithm for Rendering Space-Filling Molecule Pictures. J. Mol. Graph. 6, 219-220.
3. Cao, W., Lu, J., Welch, S. G., Williams, R. A. and Barany, F. (1998) Cloning and thermostability of TaqI endonuclease isoschizomers from thermus species SM32 and Thermus filiformis TOKGA1. Biochem. J. 333, 425-431.
4. Chan, M. K., Mukund, S., Kletzin, A., Adams, M. W. W. and Rees, D. C. (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredozin oxidoreductase. Science 267, 1463-1469.
5. Daniel, R. M., Cowan, D. A., Morgan, H. W. and Curran, M. P. (1982) A correlation between protein thermostability and resistance to proteolysis. Biochem. J. 207, 641-644.
6. Day, M. W., Hsu, B. T., Joshu-Tor, L., Park, J., Zhou, Z. H., Adams, M. W. W. and Rees, D. C. (1992) X-Ray crystal structure of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. Protein Sci. 1, 1494-1507.
7. Eijsink, V. G. H., Vriend, vanden Burg, G. B., vander Zee, J. R. and Venema, G. (1992) Increasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of α-helices. Protein Eng. 5, 165-170.
8. Eriksson, A. E., Baase, W. A., Zhang, X. J., Heinze, D. W., Blaber, M., Baldwin, E. P. and Matthews, B. W. (1992) Response of a protein structure to cavity creating mutations and its relation to the hydrophobic effect. Science 255, 178-183.
9. Fields, P. A. and Somero, G. N. (1998) Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenoid fishes. Proc. Natl. Acad. Sci. USA 95, 11476-11481.
10. Fleming, T. and Littlechild, J. (1997) Sequence and structural comparison of thermophilic phophoglycerate kinases with a mesophilic equivalent. Comp. Biochem. Physiol. 118A, 439-451.
11. Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y. and Oshima, T. (1991) Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution. J. Mol. Biol. 222, 725-738.
12. Kim, Y. K., Choi, I. G., Nam, W. and Yu, Y. G. (2000) Identification of a mature form and Characterization of Thermostability of a Serine-type Protease from Aquifex pyrophilus. J. Biochem. Mol. Biol. 33, 493-498.
13. Kim, S. Y., Hwang, K. Y., Kim, S. H., Sung, H. C., Han, Y. S. and Cho, Y. (1999) Structural basis for cold adaptation. J. Biol. Chem. 274, 11761-11767.
14. Kraulis, P. J. (1991) MOLSCRIPT: A Program to Produce Both Detailed and Schematic Plots of Protein Structures. J. Appl. Crystal. (1991) 24, 946-950.
15. Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crylstallogr. 26, 47-60.
16. Lim, W. A. and Sauer, R. T. (1989) Alternative packing arrangements in the hydrophobic core of l repressor. Nature 339, 31-36.
17. Matsumura, M., Becktel, W. J. and Matthews, B. W. (1988) Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature 334, 406-410.
18. Mitchinson, C. and Wells, J. A. (1989) Protein engineering of disulfide bonds in subtilisin BPN'. Biochemistry 28, 4807-4815.
19. Nakamura, S., Tanaka, T., Yada, R. Y. and Nakai, S. (1997) Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix. Protein Eng. 10, 1263-1269.
20. Panasik, N, Brenchley, J. E. and Farber, G. K. (2000) Distributions of structural features contributing to thermostability in mesophilic and thermophilic a/b barrel glycosyl hydrolyses. Biochim. Biophys. Acta 1543, 189-201.
21. Perutz, M. F. and Raidt, H. (1975) Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2. Nature 255, 256-259.
22. Russell, R. J. M., Ferguson, J. M. C., Hough, D. W., Danson, M. J. and Taylor, G. L. (1997) The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiousus at 1.9 Å resolution. Biochemistry 36, 9983-9994.
23. Russell, R. J. M., Gerike, U., Danson, M. J., Hough, D. W. and Taylor, G. L. (1998) Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 6, 351-361.
24. Sali, A. and Blundell, T. L. (1993) Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
25. Sandberg, W. S. and Terwillinger, T. C. (1991) Influence of interior packing and hydrophobicity on the stability of a protein. Proc. Natl. Acad. Sci. USA 88, 1706-1710.
26. Scandurra, R., Consalvi, V., Chiaraluce, R., Politi, L. and Engel P. C. (1998) Protein thermostability in extremophiles. Biochimie 80, 933-941.
27. Shortle, D. (1992) Mutational studies of protein structures and their stabilities. Q. Rev. Biophys. 25, 205-250.
28. Sippl, M. J. (1993) Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures. J. Compu.-Aided. Mol. Des. 7, 473-501.
29. Takagi, H., Hirai, K., Maeda, Y., Matsuzawa, H. and Nakamori, S. J. (2000) Engineering subtilisin E for enhanced stability and activity in polar organic solvents. J. Biochem. 127, 617-625.
30. Takagi, H., Takahashi, T., Momose, H., Inouye, M., Maeda, Y., Matsuzawa, H. and Ohta, T. (1990) Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease. J. Biol. Chem. 265, 6874-6878.
31. Teplyakov, A. V., Kuranova, I. P., Harutyunyan, E. H., Frommel, C. and Hohne, W. E. (1989) Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2 A resolution. FEBS Lett. 244, 208-212.
32. Urfer, R. and Kirschner, K. (1992) The importance of surface loops for stabilizing an eightfold a/b barrel protein. Protein Sci. 1, 31-45.
33. Vogt, G., Woell, S. and Argos, P. (1997) Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269, 631-643.
34. Vriend, G. and Sander, C. (1993) Quality-Control of Protein Models-Directional Atomic Contact Analysis. J. Appl. Crystallogr. 26, 47-60.
35. Wallon, G., Kryger, G., Lovett, S. T., Oshima, T., Ringe, D. and Petsko, G. A. (1997) Crystal structure of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. J. Mol. Biol. 266, 1016-1031.
36. Wells, J. A. and Powers, D. B. (1986) In vivo formation and stability of engineered disulfide bonds in subtilisin. J. Biol. Chem. 261, 6564-6570.
37. Yip, K. S., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R. and Consalvi, V. (1995) The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3, 1147-1158.
38. Yutani, K., Ogasahara, K., Tsujita, T. and Sugino, Y. (1987) Dependence of conformational stability on hydrophobicity of the amino acid residues in a series of variant proteins substituted at a unique position of tryptophan synthase a subunit. Proc. Natl. Acad. Sci. USA 84, 4441-4444.
39. Zavodszky, P., Kardos, J., Svingor, A. and Petsko, G. A. (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. USA 95, 7406-7411.