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A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes

Nature Structural Biology volume 4, pages 519–522 (1997)Cite this article

A Corrigendum to this article was published on 01 October 1997

A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 Å). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

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References

  1. Hibbert, F. & Emsley, J. Adv. Phys. Org. Chem. 26, 255–379 (1990).

    CAS  Google Scholar 

  2. Cleland, W.W. & Krevoy, M.M. Science 264, 1887–1890 (1994).

    Article  CAS  Google Scholar 

  3. Gerlt, J.A. & Gassman, P.G. Biochemistry 32, 11943–11952 (1993).

    Article  CAS  Google Scholar 

  4. Frey, P.A. & Whitt, S.A. & J.B., Tobin, J.B. Science 264, 1927–1930 (1994).

    Article  CAS  Google Scholar 

  5. Warshel, A. & Papazyan, A. Proc. Natl. Acad. Sci. U.S.A. 93, 13665–13670 (1996).

    Article  CAS  Google Scholar 

  6. Shan, S., Loh, S. & Herschlag, D. Science 272, 97–101 (1996).

    Article  CAS  Google Scholar 

  7. Tronrud, D.E., Holden, H.M. & Matthews, B.W. Science 235, 571–574 (1987).

    Article  CAS  Google Scholar 

  8. Luecke, H. & Quiocho, F.A. Nature 347, 402–406 (1990).

    Article  CAS  Google Scholar 

  9. Kirn, H. & Lipscomb, W.N. Biochemistry 30, 8171–8180 (1991).

    Article  Google Scholar 

  10. Fraser, M.E., Strynadka, N.C., Bartlett, P.A., Hanson, J.E. & James, M.N. Biochemistry 31, 5201–5214 (1992).

    Article  CAS  Google Scholar 

  11. Usher, K.C., Remington, J., Martin, D.P. & Drueckhamer, D. G. Biochemisitry 33, 7753–7759 (1994).

    Article  CAS  Google Scholar 

  12. Konnert, J.H. & Hendrickson, W.A. Acta Crystallogr. A 36, 344–350 (1980).

    Article  Google Scholar 

  13. Brünger, A.T. X-PLOR Version 3.1 Manual (Yale University Press, New Haven, Connecticut; 1992).

  14. Wang, Z., Choudhary, A., Ledvina, P.S. & Quiocho, F.A. J.Biol. Chem. 269, 25091–25094 (1994).

    CAS  PubMed  Google Scholar 

  15. Yao, N., Ledvina, P.S., Choudhary, A. & Quiocho, F.A. Biochemistry 35, 2079–2085 (1996).

    Article  CAS  Google Scholar 

  16. Sheldrick, G.M. & Schneider, T. Meths Enz. in press.

  17. Dauter, Z., Lamzin, V.S. & Wilson, K.S. Curr. Opin. Struct. Biol. 5, 784–790 (1995).

    Article  CAS  Google Scholar 

  18. Otwinowski, Z. in Data Collection and Processing (eds Sawyer, L, N. Isaacs, N. W. & Bailey S.) 55–62 (SERC Daresbury Laboratory, Warrington; 1993).

    Google Scholar 

  19. Sack, J.S. J. Mol. Graphics 6, 224–225 (1988).

    Article  Google Scholar 

  20. Pardee, A.B. et al., J. Biol. Chem. 241, 3962–3969 (1966).

    CAS  PubMed  Google Scholar 

  21. Jacobson, B.L. & Quiocho, F.A. J. Mol. Biol. 204, 783–787 (1988).

    Article  CAS  Google Scholar 

  22. Medveczky, N. & Rosenberg, H. Biochim. Biophys. Acta 192, 369–371 (1969).

    Article  CAS  Google Scholar 

  23. Medveczky, N. & Rosenberg, H., 211, 158–168 (1970).

  24. Brune, M., Hunter, J.L., Corrie, J.E.T. & Webb, M.R. Biochemistry 33, 8262–8271 (1994).

    Article  CAS  Google Scholar 

  25. Ferrin, T.E. et al. J. Mol. Graphics 6, 13–27 (1988)

    Article  CAS  Google Scholar 

  26. Burnett, M.N. & Johnson, C.K., Oak Ridge National Laboratory Report ORNL-6895 (1996).

Download references

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Authors and Affiliations

  1. Structural and Computational Biology and Molecular Biophysics Program, Baylor College of Medicine, Houston, Texas, 77030, USA

    Zhongmin Wang & Florante A. Quiocho

  2. Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas, 77030, USA

    Florante A. Quiocho

  3. Department of Biochemistry, Baylor College of Medicine, Houston, Texas, 77030, USA

    Nanhua Yao & Florante A. Quiocho

  4. Stanford Synchrotron Radiation Laboratory, MS 69, Stanford, California, 94305, USA

    Hartmut Luecke

  5. Department of Molecular Biology and Biochemistry, University of California, Irvine, California, 92717, USA

    Hartmut Luecke

  6. Macromolecular Crystallography, Schering-Plough Research Institute, Kenilworth, New Jersey, 07033, USA

    Nanhua Yao

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  1. Zhongmin Wang
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  2. Hartmut Luecke
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  3. Nanhua Yao
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  4. Florante A. Quiocho
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Wang, Z., Luecke, H., Yao, N. et al. A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes. Nat Struct Mol Biol 4, 519–522 (1997). https://doi.org/10.1038/nsb0797-519

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