Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution

Biochemistry

Volumn 35, Issue 8, 1996, Pages 2597-2609

  Tanner, John J ^a   Hecht, Ralph M ^a   Krause, Kurt L ^a  

^a UNIVERSITY OF HOUSTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

ARTICLE; CRYSTALLOGRAPHY; ENZYME STABILITY; ENZYME STRUCTURE; PRIORITY JOURNAL; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTROCHEMISTRY; ENZYME STABILITY; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS; THERMUS;

BACTERIA (MICROORGANISMS); THERMUS AQUATICUS;

EID: 0029936488     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi951988q     Document Type: Article

References (69)

1. Abola, E. E., Bernstein, F. C., Bryant, S. H., Koetzle, T. F., & Weng, J. (1987) in Crystallographic databases - Information content software systems, scientific applications (Allen, F. H., Bergerhoff, G., & Sievers, R., Eds,) pp 107-132, Data Commission of the International Union of Crystallography, Bonn/ Cambridge/Chester.
2. Adams, M. W. W., & Kelly, R. M. (1994) Bioorg. Med. Chem. 2, 659-667.
3. Alber, T. (1989) Annu. Rev. Biochem. 58, 765-798.
4. Anderson, D. E., Becktel, W. J., & Dahlquist, F. W. (1990) Biochemistry 29, 765-784.
5. Argos, P., Rossmann, M. G., Grau, U. M., Zuber, H., Frank, G., & Tratschin, J. D. (1979) Biochemistry 18, 5698-5703.
6. Baker, E. N., & Hubbard, R. E. (1984) Prog. Biophys. Mol. Biol. 44, 97-179.
7. Biro, J., Fabry, S., Dietmaier, W., Bogedain, C., & Hensel, R. (1990) FEBS Lett. 275, 130-134.
8. Brünger, A. T. (1992) X-PLOR version 3.1, A system for x-ray crystallography and NMR, Yale University Press, New Haven.
9. Chan, M. K., Mukund, S., Kietzin, A., Adams, M. W. W., & Rees, D. C. (1995) Science 267, 1463-1469.
10. Dao-pin, S., Sauer, U., Nicholson, H., & Matthews, B. W. (1991) Biochemistry 30, 7142-7153.
11. Davies, G. J., Gamblin, S. J., Littlechild, J. A., & Watson, H. C. (1993) Proteins: Struct, Funct., Genet. 15, 283-289.
12. Day, M. W., Hsu, B. T., Joshua-Tor, L., Park, J.-B., Zhou, Z. H., Adams, M. W. W., & Rees, D. C. (1992) Protein Sci. 1, 1494-1507.
13. Devereux, J., Haeberli, P., & Smithies, O. (1984) Nucleic Acids Res. 12, 387-395.
14. Engh, R. A., & Huber, R. (1991) Acta Crystallogr. A47, 392-400.
15. Fabry, S., Lang, J., Niermann, T., Vingron, M., & Hensel, R. (1989) Eur. J. Biochem. 179, 405-413.
16. Fersht, A. R. (1972) J. Mol. Biol. 64, 497-509.
17. Fersht, A. R., & Serrano, L. (1993) Curr. Opin. Struct. Biol. 3, 75-83.
18. Furey, W., & Swaminathan, S. (1995) in Macromolecular Crystallography, A Volume of Methods in Enzymology (Carter, C., & Sweet, R., Eds.) Academic Press, Orlando, FL.
19. Griffith, J. P., Lee, B., Murdock, A. L., & Amelunxen, R. E. (1983) J. Mol. Biol. 169, 963-974.
20. Hendsch, Z. S., & Tidor, B. (1994) Protein Sci. 3, 211-226.
21. Higashi, T. (1990) PROCESS: A program for indexing and processing R-AXIS II imaging plate data, Rigaku Corp., Tokyo.
22. Honig, B., & Nicholls, A. (1995) Science 268, 1144-1149.
23. Honka, E., Fabry, S., Niermann, T., Palm, P., & Hensel, R. (1990) Eur. J. Biochem. 188, 623-632.
24. Horovitz, A., Serrano, L., Avron, B., Bycroft, M., & Fersht, A. R. (1990) J. Mol. Biol. 216, 1031-1044.
25. Jaenicke, R. (1991) Eur. J. Biochem. 202, 715-728.
26. Jecht, M., Tomschy, A., Kirschner, K., & Jaenicke, R. (1994) Protein Sci. 3, 411-418.
27. Jones, T. A. (1978) J. Appl. Crystallogr. 11, 268-272.
28. Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) Acta Crystallogr. A47, 110-119.
29. Kelly, C. A., Bishiyama, M., Ohnishi, Y., Beppu, T., & Birktoft, J. J. (1993) Biochemistry 32, 3913-3922.
30. Knapp, S., Karshikoff, A., Waldkötter, K., Rüdiger, A., Antranikian, G., & Ladenstein, R. (1995) Acta. Crystallogr. D51, 395-398.
31. Korndörfer, I., Steipe, B., Huber, R., Tomschy, A., & Jaenicke, R. (1995) J. Mol. Biol. 246, 511-521.
32. Kotik, M., & Zuber, H. (1993) Eur. J. Biochem. 211, 267-280.
33. Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
34. Lin, Z.-j., Li, J., Zhang, F.-m., Song, S.-y., Yang, J., Liang, S.-j., & Tsou, C.-l. (1993) Arch. Biochem. Biophys. 302, 161-166.
35. Luzzati, P. V. (1952) Acta Crystallogr, 5, 802-810.
36. Matthews, B. W. (1991) Curr. Opin. Struct. Biol. 1, 17-21.
37. Matthews, B. W. (1995) Annu. Rev. Biochem. 62, 139-160.
38. Menendez-Arias, L., & Argos, P. (1989) J. Mol. Biol. 206, 397-406.
39. Mercer, W. D., Winn, S. I., & Watson, H. C. (1976) J. Mol. Biol. 104, 277-283.
40. Merkler, D. J., Farrington, G. K., & Wedler, F. C. (1981) Int. J. Pept. Protein Res. 18, 430-442.
41. Miller, S., Janin, J., Lesk, A. M., & Chothia, C. (1987) J. Mol. Biol. 196, 641-656.
42. Moore, W. J. (1972) Physical Chemistry, Prentice-Hall, Englewood Cliffs, NJ.
43. Moras, D., Olsen, K. W., Sabesan, M. N., Buehner, M., Ford, G. C., & Rossmann, M. G. (1975) J. Biol. Chem. 250, 9137-9162.
44. Murthy, M. R. N., Garavito, R. M., Johnson, J. E., & Rossmann, M. G. (1980) J. Mol. Biol. 138, 859-872.
45. Nichoils, A., & Honig, B. (1992) GRASP: graphical representation and analysis of surface properties, Columbia University, New York.
46. Nicholson, H., Becktel, W. J., & Matthews, B. W. (1988) Nature 336, 651-656.
47. Perutz, M. F., & Raidt, H. (1975) Nature 255, 256-259.
48. Rees, D. C., & Adams, M. W. W. (1995) Structure 3, 251-254.
49. Rehaber, V., & Jaenicke, R. (1992) J. Biol. Chem. 267, 10999-11006.
50. Sali, D., Bycroft, M., & Fersht, A. R. (1991) J. Mol. Biol. 220, 779-788.
51. Schläpfer, B. S., & Zuber, H. (1992) Gene 122, 53-62.
52. Schueler, O., & Margalit, H. (1995) J. Mol. Biol. 248, 125-135.
53. Shirley, B. A., Stanssens, P., Hahn, U., & Pace, C. N. (1992) Biochemistry 31, 725-732.
54. Skarzynski, T., & Wonacot, A. J. (1988) J. Mol. Biol. 203, 1097-1118.
55. Skarzynski, T., Moody, P. C. E., & Wonacott, A. J. (1987) J. Mol. Biol. 193, 171-187.
56. Sterner, R., Vogl, T., Hinz, H.-J., Penz, F., Hoff, R., Föll, R., & Decker, H. (1995) FEBS Lett. 364, 9-12.
57. Suzuki, K., & Harris, J. I. (1971) FEBS Lett. 13, 217-220.
58. Tanner, J., & Krause, K. L. (1994) Rigaku J. 11, 4-10.
59. Tanner, J., Hecht, R. M., Pisegna, M., Seth, D. M., & Krause, K. L. (1994) Acta Crystallogr. D50, 744-748.
60. Tomschy, A., Bohm, G., & Jaenicke, R. (1994) Protein Eng. 7, 1471-1478.
61. Tomschy, A., Glockshuber, R., & Jaenicke. R. (1993) Eur. J. Biochem. 214, 43-50.
62. Vellieux, F. M. D., Hajdu, J., Verlinde, C. L. M. J., Groendijk, H., Read, R. J., Greenhough, T. J., Campbell, J. W., Kalk, K. H., Littlechild, J. A., Watson, H. C., & Hol, W. G. J. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 2355-2359.
63. Waldburger, C. D., Schildbach, J. F., & Sauer, R. T. (1995) Nat. Struct. Biol. 2, 122-128.
64. Walker, J. E., Wonacott, A. J., & Harris, J. I. (1980) Eur. J. Biochem. 108, 581-586.
65. Watanabe, K., Masuda. T., Ohashi, H., Mihara, H., & Suzuki, Y. (1994) Eur. J. Biochem. 226, 277-283.
66. Yang, A.-S., Sharp, K. A., & Honig, B. (1992) J. Mol. Biol. 227, 889-900.
67. Yip, K. S. P., Baker, P. J., Britton, K. L., Engel, P. C., Rice, D. W., Sedelnikova, S. E., Stillman, T. J., Pasquo, A., Chiaraluce, R., Consalvi, V., & Scandurra, R. (1995) Acta. Crystallogr. D51, 240-242.
68. Zuber, H. (1981) in Structural and functional aspects of enzyme catalysis (Eggerer, H., & Huber, R., Eds.) pp 114-127, Springer-Verlag, Berlin.
69. Zwickl, P., Fabry, S., Bogedain, C., Haas, A., & Hensel, R. (1990) J. Bacteriol. 172, 4329-4338.