Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu·GDP and aurodox

Journal of Biological Chemistry

Volumn 276, Issue 20, 2001, Pages 17149-17155

  Vogeley, Lutz ^a   Palm, Gottfried J ^a   Mesters, Jeroen R ^a   Hilgenfeld, Rolf ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BIOSYNTHESIS; CATALYSIS; CONFORMATIONS; CRYSTAL STRUCTURE; HYDROLYSIS;

ELONGATION FACTORS;

BIOCHEMISTRY;

1 METHYLMOCIMYCIN; AMINOACYL TRANSFER RNA; ANTIBIOTIC AGENT; DIPYRONE; ELONGATION FACTOR TS; ELONGATION FACTOR TU; GOLDINOIC ACID; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HISTIDINE; MOCIMYCIN; TETRAHYDROFURAN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; GUANYLYLIMIDODIPHOSPHATE; LEUCINE; RECOMBINANT PROTEIN; TYROSINE;

ANIMAL CELL; ANTIBIOTIC RESISTANCE; ANTIMICROBIAL ACTIVITY; ARTICLE; CATALYSIS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG PROTEIN BINDING; GENE MUTATION; HYDROLYSIS; NONHUMAN; OPTICAL RESOLUTION; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REACTION ANALYSIS; RIBOSOME; RNA BINDING; STRUCTURE ANALYSIS; THERMUS THERMOPHILUS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; METABOLISM; PROTEIN CONFORMATION;

ANIMALIA; NEGIBACTERIA; THERMUS; THERMUS THERMOPHILUS;

ANTI-BACTERIAL AGENTS; AURODOX; BINDING SITES; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; GUANYLYL IMIDODIPHOSPHATE; LEUCINE; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PEPTIDE ELONGATION FACTOR TU; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; THERMUS THERMOPHILUS; TYROSINE;

EID: 0035907234     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M100017200     Document Type: Article

References (50)

1. Parmeggiani, A., and Sander, G. (1980) Top. Antibiot. Chem. 5, 165-221
2. Parmeggiani, A., and Swart, G. W. M. (1985) Annu. Rev. Microbiol. 39, 557-577
3. Chinali, G. (1981) J. Antibiot. (Tokyo) 34, 1039-1045
4. Wolf, H., Chinali, G., and Parmeggiani, A. (1974) Proc. Natl. Acad. Sci. U. S. A. 71, 4910-4914
5. Berchtold, H., Reshetnikova, L., Reiser, C. O. A., Schirmer, N. K., Sprinzl, M., and Hilgenfeld, R. (1993) Nature 365, 126-132
6. Kjeldgaard, M., Nissen, P., Thirup, S., and Nyborg, J. (1993) Structure 1, 35-50
7. Abel, K., Yoder, M., Hilgenfeld, R., and Jurnak, F. (1996) Structure 4, 1153-1159
8. Polekhina, G., Thirup, S., Kjeldgaard, M., Nissen, P., Lippmann, C., and Nyborg, J. (1996) Structure 4, 1141-1151
9. Pingoud, A., Urbanke, C., Wolf, H., and Maass, G. (1978) Eur. J. Biochem. 86, 153-157
10. Abrahams, J. P., van Raaij, M. J., Ott, G., Kraal, B., and Bosch, L. (1991) Biochemistry 30, 6705-6710
11. Douglass, J., and Blumenthal, T. (1979) J. Biol. Chem. 254, 5383-5387
12. Abrahams, J. P., Kraal, B., Bosch, L. (1988) Nucleic Acids Res. 16, 10099-10108
13. Alexander, C., Bilgin, N., Lindschau, C., Mesters, J. R., Kraal, B., Hilgenfeld, R., Erdmann, V. A., and Lippmann, C. (1995) J. Biol. Chem. 270, 14541-14547
14. Kristensen, O., Reshetnikova, L., Nissen, P., Siboska, G., Thirup, S., and Nyborg, J. (1996) FEBS Lett. 399, 59-62
15. Heffron, S. E., and Jurnak, F. (2000) Biochemistry 39, 37-45
16. Zeidler, W., Kreutzer, R., and Sprinzl, M. (1993) FEBS Lett. 319, 185-188
17. Mesters, J. R., Zeef, L. A. H., Hilgenfeld, R., de Graaf, J. M., Kraal, B., and Bosch, L. (1994) EMBO J. 13, 4877-4885
18. Abdulkarim, F., Liljas, L., and Hughes, D. (1994) FEBS Lett. 352, 118-122
19. Duisterwinkel, F. J., de Graaf, J. M., Kraal, B., and Bosch, L. (1981) FEBS Lett. 131, 89-93
20. Duisterwinkel, F. J., Kraal, B., de Graaf, J. M., Talens, A., Bosch, L., Swart, G. W. M., Parmeggiani, A., La Cour, T. F. M., Nyborg, J., and Clark, B. F. C. (1984) EMBO J. 3, 113-120
21. Maehr, H., Leach, M., Williams, T. H., and Blount, J. F. (1980) Can. J. Chem. 58, 501-526
22. Blank, J., Grillenbeck, N. W., Kreutzer, R., and Sprinzl, M. (1995) Protein Expression Purif 6, 637-645
23. Ravelli, R. R. G., Sweet, R. M., Skinner, J. M., and Duisenberg, A. J. M. (1997) J. Appl. Crystallogr. 30, 551-554
24. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
25. Collaborative Computational Project Number 4 (1994) Acta Crystallogr. Sec. D 50, 760-763
26. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497
27. Navaza, J. (1994) Acta Crystallogr. Sec. A 50, 157-163
28. Brunger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuzewski, J., Nilges, N., Pannu, N. S., Read, R. J., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sec. D 54, 905-921
29. Brünger, A. T. (1992) Nature 355, 472-475
30. Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sec. A 47, 110-119
31. Kleywegt, G. J., and Jones, T. A. (1998) Acta Crystallogr. Sec. D 54, 1119-1131
32. Cohen, G. E. (1997) J. Appl. Crystallogr. 30, 1160-1161
33. Kjeldgaard, M., and Nyborg, J. (1992) J. Mol. Biol. 223, 721-742
34. Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F. C., and Nyborg, J. (1995) Science 270, 1464-1471
35. Nissen, P., Thirup, S., Kjeldgaard, M., and Nyborg, J. (1999) Structure 7, 143-156
36. Hilgenfeld, R., Mesters, J. R., and Hogg, T. (2000) in The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions (Garrett, R. A., Douthwaite, S. R., Liljas, A., Matheson, A. T., Moore, P. B., and Noller, A. F., eds) pp. 347-357, American Society for Microbiology Press, Washington, D. C.
37. Fasano, O., Bruns, W., Crechet, J. B., Sander, G., and Parmeggiani, A. (1978) Eur. J. Biochem. 89, 557-565
38. Song, H., Parsons, M. R., Rowsell, S., Leonard, G., and Phillips, S. E. V. (1999) J. Mol. Biol. 285, 1245-1256
39. Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., and Wittinghofer, A. (1997) Science 277, 333-338
40. Landini, P., Soffientini, A., Monti, F., Lociuro, S., Marzorati, E., and Islam, K. (1996) Biochemistry 35, 15288-15294
41. Van Noort, J. M., Kraal, B., Bosch, L., La Cour, T. F., Nyborg, J., and Clark, B. F. (1984) Proc. Natl. Acad. Sci. U. S. A. 81, 3969-3972
42. Kawashima, T., Bethet-Colominas, C., Wulff, M., Cusack, S., and Leberman, R. (1996) Nature 379, 511-518
43. Wang, Y., Jiang, Y., Meyering-Voss, M., Sprinzl, M., and Sigler, P. B. (1997) Nat. Struct. Biol. 4, 650-656
44. Wolf, H., Chinali, G., and Parmeggiani, A. (1977) Eur. J. Biochem. 75, 67-75
45. Stout, G. H., and Jensen, L. H. (1968) X-ray Structure Determination: A Practical Guide, p. 402, Macmillan, New York
46. Weiss, M. S., and Hilgenfeld, R. (1997) J. Appl. Crystallogr. 30, 203-205
47. Diederichs, K., and Karplus, P. A. (1997) Nat. Struct. Biol. 4, 269-275
48. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
49. Esnouf, R. M. (1997) J. Mol. Graphics 15, 132-134
50. Merrit, E. A., and Murphy, M. E. P. (1994) Acta Crystallogr. Sec. D 50, 869-873