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Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution

Nature volume 271, pages 626–630 (1978)Cite this article

Abstract

The structure determination of pyruvate kinase shows that each subunit of the tetrameric molecule consists of three domains. The largest of these domains has a remarkable similarity to the structure of triosephosphate isomerase. Another domain shows similarities to many other nucleotide binding proteins. We discuss these similarities and their implications for current arguments on protein taxonomy and evolution.

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References

  1. Arndt, U. W., Champness, J. N., Phizackerley, R. P. & Wonacott, A. J. J. appl. Crystallogr. 6, 457–463 (1973).

    Article  CAS  Google Scholar 

  2. Dayhoff, M. O., Hunt, L. T., McLaughlin, P. J. & Jones, D. D. Atlas of Protein Sequence and Structure 5, 17–30 (1972).

    Google Scholar 

  3. Hartley, B. S. Phil. Trans. R. Soc. B 257, 77–78 (1970).

    Article  CAS  Google Scholar 

  4. Richardson, J. S. Proc. natn. Acad. Sci., U.S.A. 73, 2619–2623 (1976).

    Article  ADS  CAS  Google Scholar 

  5. Sternberg, M. J. E. & Thornton, J. M. J. molec. Biol. 105, 367–382 (1976).

    Article  CAS  Google Scholar 

  6. Rossmann, M. G., Moras, D. & Olsen, K. W. Nature 250, 194–199 (1974).

    Article  ADS  CAS  Google Scholar 

  7. Ohlsson, I., Nordström, B. & Brändén, C-I. J. molec. Biol. 89, 339–354 (1974).

    Article  CAS  Google Scholar 

  8. Eventoff, W. & Rossmann, M. G. in CRC Critical Reviews of Biochemistry (ed. Fasman, G. D.), vol. 3, 111–140 (CRC Press, Cleveland, 1975).

    Google Scholar 

  9. Banner, D. W. et al. Nature 255, 609–614 (1975).

    Article  ADS  CAS  Google Scholar 

  10. Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C. & Wilson, I. A. Biochem. biophys. Res. Commun. 72, 146–155 (1976).

    Article  CAS  Google Scholar 

  11. Blake, C. C. F. & Evans, P. R. J. molec. Biol. 84, 585–601 (1974).

    Article  CAS  Google Scholar 

  12. Bryant, T. N., Watson, H. C. & Wendell, P. L. Nature 247, 14–17 (1974).

    Article  ADS  CAS  Google Scholar 

  13. Schulz, G. E., Elzinga, M., Marx, F. & Schirmer, R. H. Nature 250, 120–123 (1974).

    Article  ADS  CAS  Google Scholar 

  14. Steitz, T. A., Fletterick, R. J., Anderson, W. F. & Anderson, C. M. J. molec. Biol. 104, 197–222 (1976).

    Article  CAS  Google Scholar 

  15. Stammers, D. K. & Muirhead, H. J. molec. Biol. 112, 309–316 (1977).

    Article  CAS  Google Scholar 

  16. Rossmann, M. G. & Argos, P. J. molec. Biol. 105, 75–95 (1976).

    Article  CAS  Google Scholar 

  17. Levitt, M. & Chothia, C. Nature 261, 552–558 (1976).

    Article  ADS  CAS  Google Scholar 

  18. Stammers, D. K. & Muirhead, H. J. molec. Biol. 95, 213–225 (1975).

    Article  CAS  Google Scholar 

  19. Rose, I. A. & Rieder, S. V. J. biol. Chem. 234, 1007–1010 (1959).

    PubMed  Google Scholar 

  20. Rose, I. A. Brookhaven Synp. Biol. 15, 293–309 (1962).

    CAS  Google Scholar 

  21. Rose, I. A. J. biol. Chem. 235, 1170–1177 (1960).

    CAS  PubMed  Google Scholar 

  22. Schulz, G. E. & Schirmer, R. H. Nature 250, 142–144 (1974).

    Article  ADS  CAS  Google Scholar 

  23. Rossmann, M. G. & Argos, P. J. biol. Chem. 250, 7525–7532 (1975).

    CAS  Google Scholar 

  24. Rao, S. T. & Rossmann, M. G. J. molec. Biol. 76, 241–256 (1973).

    Article  CAS  Google Scholar 

  25. Robinson, J. L. & Rose, I. A. J. biol. Chem. 247, 1096–1105 (1972).

    CAS  PubMed  Google Scholar 

  26. Phillips, D. C., Rivers, P. S., Sternberg, M. J. E., Thornton, J. M. & Wilson, I. A. Biochem. Soc. Trans. 5, 642–647 (1977).

    Article  CAS  Google Scholar 

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Author notes

  1. Michael Levine

    Present address: Department of Physiology, University of Bristol, Bristol, UK

  2. David K. Stammers

    Present address: The Wellcome Research Laboratories, Beckenham, Kent, UK

Authors and Affiliations

  1. Molecular Enzymology Laboratory, Department of Biochemistry, University of Bristol, Bristol, UK

    Michael Levine, Hilary Muirhead, David K. Stammers & David I. Stuart

Authors
  1. Michael Levine
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  2. Hilary Muirhead
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  3. David K. Stammers
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  4. David I. Stuart
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Levine, M., Muirhead, H., Stammers, D. et al. Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution. Nature 271, 626–630 (1978). https://doi.org/10.1038/271626a0

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