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Biophysics

Relating dynamics to function

Nature volume 400, pages 221–222 (1999)Cite this article

Movement at the molecular level is essential for macromolecular function. Nonetheless, our images of proteins are dominated by static, three-dimensional structures that give only snapshots of the allowable conformations. One method for studying the structural dynamics of macromolecules in solution is NMR spectroscopy, which is providing increasingly detailed descriptions of the motional parameters in proteins1. But it is not straightforward to correlate molecular motions with protein activities, and a central question remains — how do dynamics relate to function?

On page 289 of this issue, Feher and Cavanagh2 give an insight into this problem with their NMR dynamics study, which characterizes movements in Spo0F, a response-regulator protein involved in a phospho-relay signal-transduction pathway in Bacillus subtilis. Feher and Cavanagh find that amino-acid residues moving on microsecond to millisecond timescales in Spo0F correspond to residues that have previously been identified as important in mediating interactions with three other signalling partners3,4. This study adds to the growing list of cases where conformational dynamics are correlated with proteinprotein interaction surfaces.

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Figure 1: Dynamic regions in response-regulator proteins.

References

  1. Kay, L. E. Nature Struct. Biol. NMR Suppl. 513–517 (1998).

    Google Scholar 

  2. Feher, V. A. & Cavanagh, J. Nature 400, 289–293 (1999).

    Article  ADS  CAS  Google Scholar 

  3. Tzeng, Y.-L. et al. Biochemistry 37, 16538–16545 (1998).

    Google Scholar 

  4. Tzeng, Y.-L. & Hoch, J. A. J. Mol. Biol. 272, 200–212 (1997).

    Google Scholar 

  5. Hoch, J. A. & Silhavy, T. J. Two-Component Signal Transduction (Am. Soc. Microbiol. Press, Washington DC, 1995).

  6. Burbulys, D., Trach, K. A. & Hoch, J. A. Cell 64, 545–552 (1991).

    Google Scholar 

  7. Clore, G. M. et al. J. Am. Chem. Soc. 112, 4989–4991 (1990).

    Google Scholar 

  8. Lowry, D. F. et al. J. Biol. Chem. 269, 26358–26362 (1994).

    Google Scholar 

  9. Nohaile, M. et al. J. Mol. Biol. 273, 299–316 (1997).

    Google Scholar 

  10. Varughese, K. I., Sen, U., Zapf, J., Madhusudan, M. & Hoch, J. Am. Crystallogr. Assoc. Meeting Abstr. 40 (1999).

  11. Kern, D. et al. Keystone Symp. Frontiers of NMR in Mol. Biol. VI Abstr. 76 (1999).

  12. Goudreau, P. N. & Stock, A. M. Curr. Opin. Microbiol. 1, 160–169 (1998).

    Google Scholar 

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  1. Department of Biochemistry, Center for Advanced Biotechnology and Medicine, and University of Medicine and Dentistry of New Jersey, 679 Hoes Lane, Piscataway, 08854-5638, New Jersey, USA

    Ann Stock

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Stock, A. Relating dynamics to function. Nature 400, 221–222 (1999). https://doi.org/10.1038/22233

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