Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water - NOE NMR experiments

Biochemistry

Volumn 42, Issue 38, 2003, Pages 11100-11108

  Cai, Sheng ^a   Stevens, Shawn Y ^a   Budor, Andrew P ^a   Zuiderweg, Erik R P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SOLVENT INTERATIONS;

BACTERIOLOGY; BINDING ENERGY; FREE ENERGY; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; SOLVENTS;

BIOCHEMISTRY;

ASPARAGINYLARGINYLLEUCYLLEUCYLLEUCYLTHREONYLGLYCINE; BACTERIAL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70; PEPTIDE; PROTEIN DNAK; SOLVENT; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING AFFINITY; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; HSP70 HEAT-SHOCK PROTEINS; HYDROPHOBICITY; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; SUBSTRATE SPECIFICITY; WATER;

BACTERIA (MICROORGANISMS);

EID: 0141456396     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030097c     Document Type: Article

References (50)

1. Yamano, A., Heo, N. H., and Teeter, M. M. (1997) J. Biol. Chem. 272, 9597-9600.
2. García de la Torre, J., Huertas H. L., and Carrasco B. (2000) Biophys. J. 78, 719-730.
3. Hendrick, J. P., Langer, T., Davis, T. A., Hartl, F. U., and Wiedmann, M. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 10216-10220.
4. Craig, E. A., Gambill, B. D., and Nelson, R. J. (1993) Microbiol. Rev. 57, 402-414.
5. Martin, J., and Hartl, F. U. (1997) Curr. Opin. Struct. Biol. 7, 41-52.
6. Bukau, B., and Horwich, A. L. (1998) Cell 92, 351-366.
7. Wickner, S., Maurizi, M., and Gottesman, S. (1999) Science 286, 1888-1893.
8. Szabo, A., Langer, T., Schroder, H., Flanagan, J., Bukau, B., and Hartl, F. U. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10345-10349.
9. Mayer, M. P., Rudiger, S., and Bukau, B. (2000) Biol. Chem. 381, 877-885.
10. Hubbard, T. J., and Sander, C. (1991) Protein Eng. 4, 711-717.
11. Slepenkov S. V., and Witt, S. N. (2002) Mol. Microbiol. 45, 1197-1206.
12. Hartl, F. U. (1996) Nature 381, 571-580.
13. Flaherty, K. M., Deluca-Flaherty, C., and McKay, D. B. (1990) Nature 346, 623-628.
14. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., and Hendrickson, W. A. (1996) Science 272, 1606-1614.
15. Pellecchia, M., Montgomery, D. L., Stevens, S. Y., Vander Kooi, C. W., Feng, H., Gierasch, L. M., and Zuiderweg, E. R. P. (2000) Nat. Struct. Biol. 7, 298-303.
16. Wang, H., Kurochkin, A. V., Pang, Y., Hu, W., Flynn, G. C., and Zuiderweg, E. R. P. (1998) Biochemistry 37, 7929-7940.
17. Morshauser, R. C., Hu, W., Wang, H., Pang, Y., Flynn, G. C., and Zuiderweg, E. R. P. (1999) J. Mol. Biol. 289, 1387-1403.
18. Stevens, S. Y., Cai, S., Pellecchia, M., and Zuiderweg, E. R. P. (2003) Protein Sci. (in press).
19. Blokzijl, W., and Engberts, J. B. F. N. (1993) Angew. Chem., Int. Ed. Engl. 32, 1545-1579.
20. Otting, G., Liepinsh, E., and Wüthrich, K. (1991) Science 254, 974-980.
21. Liepinsh, E., Rink, H., Otting, G., and Wüthrich, K. (1993) J. Biomol. NMR 3, 253-257.
22. Ernst, J. A., Clubb, R. T., Zhou, H. X., Gronenborn, A. M., and Clore, G. M. (1995) Science 267, 1813-1817.
23. Melacini, G., Kaptein, R., and Boelens, R. (1999) J. Magn. Reson. 136, 214-218.
24. Phan, A. T., Leroy, J.-L., and Guéron, M. (1999) J. Mol. Biol. 286, 505-519.
25. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293.
26. Johnson, B. A., and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614.
27. Otting, G. (1997) Prog. Nucl. Magn. Reson. Spectrosc. 31, 259-285.
28. Gemmecker, G. Jahnke, W., and Kessler, H. (1993) J. Am. Chem. Soc. 115, 11620-11621.
29. Grzesiek, S., and Bax, A. (1993) J. Biomol. NMR 3, 627-638.
30. Mori, S., Abeygunawardana, C., Van Zijl, P. C. M., and Berg, J. (1996) J. Magn. Reson. B110, 96-101.
31. Mori, S., Berg, J. M., and Van Zijl, P. C. M. (1996) J. Biomol. NMR 7, 77-81.
32. Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12593-12594.
33. Olejniczak, E. T., Gampe, R. T., and Fesik, S. W. (1986) J. Magn. Reson. 67, 28-41.
34. Massefski, W., and Redfield, A. (1988) J. Magn. Reson. 78, 150-155.
35. Fejzo, J., Westler, W. M., Macura, S., and Markley, J. L. (1991) J. Magn. Res. 92, 195-203.
36. Mori, S., Abeygunawardana, C., Johnson, M. O., and van Zijl, P. C. M. (1995) J. Magn. Reson. B108, 94-98.
37. Kay, L., Keifer, E. P., and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665.
38. Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371.
39. Cheng, Y. K., and Rossky, P. J. (1998) Nature 392, 696-699.
40. Juers, D. H., Jacobson, R. H., Wigley, D., Zhang, X. J., Huber, R. E., Tronrud, D. E., and Matthews, B. W. (2000) Protein Sci. 9, 1685-1699.
41. Melacini, G., Bonvin, A. M., Goodman, M., Boelens, R., and Kaptein, R. (2000) J. Mol. Biol. 300, 1041-1049.
42. Carey, C., Cheng, Y. K., and Rossky, P. J. (2000) Chem. Phys. 258, 415-425.
43. Yu, B., Blaber, M., Gronenborn, A. M., Clore, G. M., and Caspar, D. L. D. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 103-108.
44. Otting, G., Liepinsh, E., Halle, B., and Frey, U. (1997) Nat. Struct. Biol. 4, 396-404.
45. Buczynski, G., Slepenkov, S. V., Sehorn, M. G., and Witt, S. N. (2001) J. Biol. Chem. 276, 27231-27236.
46. Slepenkov, S. V., and Witt, S. N. (2002) Biochemistry 41, 12224-12235.
47. Scapin, G., Gordon, J. I., and Sacchettini, J. C. (1992) J. Biol. Chem. 267, 4253-4269.
48. Wiesner, S., Kurian, E., Prendergast, F. G., and Halle, B. (1999) J. Mol. Biol. 286, 233-246.
49. Brunne, R. M., Liepinsh, E., Otting, G, Wüthrich, K., and Van Gunsteren, W. F. (1993) J. Mol. Biol. 231, 1040-1048.
50. Koradi, R., Billeter, M., and Wüthrich, K. (1996) J. Mol. Graphics 14, 51-55.