Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution

A Correction to this article was published on 09 May 1996

Abstract

The crystal structure of the EF-Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 Å. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dirtier, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.

Your institute does not have access to this article

Relevant articles

Open Access articles citing this article.

Access options

Buy article

Get time limited or full article access on ReadCube.

$32.00

All prices are NET prices.

References

  1. Ertel, R., Redfield, B., Brot, N. & Weissbach, H. Archs Biochem. Biophys. 128, 331–338 (1968).

    CAS  Article  Google Scholar 

  2. Bourne, H. R., Sanders, D. A. & McCormick, F. Nature 349, 117–127 (1991).

    ADS  CAS  PubMed  Google Scholar 

  3. Lucus-Lenard, J. & Lipmann, F. Proc. natn. Acad. Sci. U.S.A. 55, 1562–1566 (1966).

    ADS  Article  Google Scholar 

  4. Weissbach, H., Miller, D. L. & Hachmann, J. Archs Biochem. Biophys. 137, 262–269 (1970).

    CAS  Article  Google Scholar 

  5. Miller, D. L. & Weissbach, H. Archs Biochem. Biophys. 141, 26–37 (1970).

    CAS  Article  Google Scholar 

  6. Leberman, R. et al. Analyt. Biochem. 104, 29–36 (1980).

    CAS  Article  PubMed  Google Scholar 

  7. Blumental, T., Landers, T. A. & Weber, K. Proc. natn. Acad. Sci. U.S.A. 69, 1313–1317 (1972).

    ADS  Article  Google Scholar 

  8. Kjeldgaard, M. & Nyborg, J. J. molec. Biol. 223, 721–742 (1992).

    CAS  Article  PubMed  Google Scholar 

  9. Kabsch, W., Gast, W. H., Schulz, G. E. & Leberman, R. J. molec. Biol. 117, 999–1012 (1977).

    CAS  Article  PubMed  Google Scholar 

  10. Pai, E. F. et al. Nature 341, 209–214 (1989).

    ADS  CAS  Article  PubMed  Google Scholar 

  11. Kjeldgaard, M., Nissen, P., Thirup, S. & Nyborg, J. Structure 1, 35–50 (1993).

    CAS  Article  PubMed  Google Scholar 

  12. Berchtold, H. et al. Nature 365, 126–132 (1993).

    ADS  CAS  Article  PubMed  Google Scholar 

  13. Jones, M. D. et al. Eur. J. Biochem. 108, 507–526 (1980).

    CAS  Article  PubMed  Google Scholar 

  14. An, G., Bendiak, D. S., Mamelak, L. A. & Friesen, J. D. Nucleic Acids Res. 9, 4163–4172 (1981).

    CAS  Article  PubMed  PubMed Central  Google Scholar 

  15. Leberman, R., Schulz, G. E. & Suck, D. FEBS Lett. 124, 279–281 (1981).

    CAS  Article  PubMed  Google Scholar 

  16. Schneider, U. dissertation, Univ. Freiburg, Germany (1983).

  17. Schick, B. & Jurnak, F. Acta crystallogr. D50, 563–568 (1994).

    CAS  Google Scholar 

  18. Kawashima, T., Berthet-Colominas, C., Cusask, S. & Leberman, R. Acta crystallogr. (in the press).

  19. Collaborative Computing Project No. 4 (SERC Daresbury Laboratory, Warrington, 1979).

  20. Arai, K.-I., Kawakita, M. & Kaziro, Y. J. biol Chem. 247, 7029–7037 (1972).

    CAS  PubMed  Google Scholar 

  21. John, J. et al. J. biol. Chem. 268, 923–929 (1993).

    CAS  PubMed  Google Scholar 

  22. Blumental, T. & Carmichael, G. C. A. Rev. Biochem. 48, 525–548 (1979).

    Article  Google Scholar 

  23. Janssen, G. M. C., van Damme, H. T. F., Kriek, J., Amons, R. & Möller, W. J. biol. Chem. 269, 32410–32417 (1994).

    Google Scholar 

  24. Boguski, M. S. & McCormick, G. Nature 366, 643–654 (1993).

    ADS  CAS  Article  PubMed  Google Scholar 

  25. Leslie, A. G. W. in Proceedings of the CCP4 Study Weekend (eds Helliwell, J. R., Machin, P. A. & Papiz, M. Z.) 39–50 (SERC Daresbury Laboratory, Warrington, 1987).

    Google Scholar 

  26. Jones, T. A., Cowan, S., Zou, J.-Y. & Kjelgaard, M. Acta crystallogr. A47, 110–119 (1990).

    Google Scholar 

  27. Jones, T. A. in Molecular Replacement (eds Dodson, E. J., Gover, S. & Wolf, W.) 92–105 (SERC Daresbury Laboratory, Warrington, 1992).

    Google Scholar 

  28. Brünger, A. T. Nature 355, 472–475 (1992).

    ADS  Article  PubMed  Google Scholar 

  29. Kraulis, P. J. appl. Crystallogr. 24, 946–950 (1991).

    Article  Google Scholar 

  30. Kabsh, W. & Sander, C. Biopolymers 22, 2577–2637 (1983).

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Kawashima, T., Berthet-Colominas, C., Wulff, M. et al. The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution. Nature 379, 511–518 (1996). https://doi.org/10.1038/379511a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/379511a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing