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.

  • Article
  • Published:

Crystal structure of the active site of ribulose-bisphosphate carboxylase

Nature volume 337, pages 229–234 (1989)Cite this article

Abstract

Ribulose-bisphosphate carboxylase catalyses the key carboxylation reaction of photosynthetic carbon fixation, but also the competing oxygenase reaction of photorespiration. The structure of the active site of ribulose-bisphosphate carboxylase described here should provide a rational basis for attempts to improve the efficiency of the enzyme by genetic engineering.

Access through your institution
Buy or subscribe

This is a preview of subscription content, access via your institution

Access options

Access through your institution

Buy this article

  • Purchase on SpringerLink
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Miziorko, H. M. & Lorimer, G. H. A. Rev. Biochem. 52, 507–535 (1983).

    Article  CAS  Google Scholar 

  2. Lorimer, G. H. & Miziorko, H. M. Biochemistry 19, 5321–5328 (1980).

    Article  CAS  Google Scholar 

  3. Lorimer, G. H. Biochemistry 20, 1236–1240 (1981).

    Article  CAS  Google Scholar 

  4. Pierce, J. & Reddy, G. S. Archs Biochem. Biophys. 245, 483–493 (1986).

    Article  CAS  Google Scholar 

  5. Schneider, G., Lindqvist, Y., Brändén, C.-I. & Lorimer, G. H. EMBO J. 5, 3409–3415 (1986).

    Article  CAS  Google Scholar 

  6. Nargang, F., McIntosh, L. & Somerville, C. R. Molec. Gen. Genet. 193, 220–224 (1984).

    Article  CAS  Google Scholar 

  7. Chapman, M. S., Suh, S. W., Cascio, D., Smith, W. W. & Eisenberg, D. Nature 329, 354–356 (1987).

    Article  ADS  CAS  Google Scholar 

  8. Schneider, G., Brändén, C.-I. & Lorimer, G. H. J. molec. Biol. 187, 141–143 (1986).

    Article  CAS  Google Scholar 

  9. Sussman, J. L., Holbrook, S. R., Church, G. M. & Kim, S.-H. Acta crystallogr. A33, 800–804 (1977).

    Article  ADS  CAS  Google Scholar 

  10. Konnert, J. H. & Hendrickson, W. A. Acta crystallogr. A36, 344–350 (1980).

    Article  ADS  CAS  Google Scholar 

  11. Jones, T. A. & Thirup, S. EMBO J. 5, 819–822 (1986).

    Article  CAS  Google Scholar 

  12. Andersson, I. & Brändén, C.-I. J. molec. Biol. 172, 363–366 (1984).

    Article  CAS  Google Scholar 

  13. Wang, B. C. Meth. Enzym. 115, 252–270 (1985).

    Article  Google Scholar 

  14. Bricogne, G. Acta crystallogr. A32, 832–847 (1976).

    Article  ADS  CAS  Google Scholar 

  15. Miziorko, H. M. & Sealy, R. C. Biochemistry 23, 479–485 (1984).

    Article  CAS  Google Scholar 

  16. Styring, S. & Brändén, R. Biochemistry 24, 6011–6019 (1985).

    Article  CAS  Google Scholar 

  17. Schloss, J. V. & Lorimer, G. H. J. biol. Chem. 257, 4691–4694 (1982).

    CAS  PubMed  Google Scholar 

  18. Pierce, J. Biochemistry 27, 1311–1315 (1988).

    Article  Google Scholar 

  19. Lorimer, G. H., Gutteridge, S. & Reddy, G. S. J. biol. Chem. (in the press).

  20. Lorimer, G. H., Gutteridge, S. & Madden, M. W. in Plant Molecular Biology (eds Wettstein, D. & Chua, N.-H.) 21–31 (Nato ASI series A, 140).

  21. Estelle, M., Hanks, J., McIntosh, L. & Somerville, C. R. J. biol. Chem. 260, 9523–9526 (1985).

    CAS  PubMed  Google Scholar 

  22. Robison, P. D., Martin, N. N. & Tabita, F. R. Biochemistry 18, 4453–4458 (1979).

    Article  CAS  Google Scholar 

  23. Hartman, F. C., Stringer, C. D. & Lee, E. H. Archs Biochem. Biophys. 232, 280–295 (1984).

    Article  CAS  Google Scholar 

  24. Hartman, F. C. et al. J. biol. Chem. 262, 3496–3501 (1987).

    CAS  PubMed  Google Scholar 

  25. Herndon, C. S., Norton, I. L. & Hartman, F. C. Biochemistry 21, 1380–1385 (1982).

    Article  CAS  Google Scholar 

  26. Lorimer, G. H. & Hartman, F. C. J. biol. Chem. 263, 6468–6471 (1988).

    CAS  PubMed  Google Scholar 

  27. Larimer, F. W., Lee, E. H., Mural, R. J., Soper, T. S. & Hartman, F. C. J. biol. Chem. 262, 15327–15329 (1987).

    CAS  PubMed  Google Scholar 

  28. Kabsch, W. & Sander, C. FEBS Lett. 155, 179–182 (1983).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, PO Box 590, Uppsala, S-75124, Sweden

    Inger Andersson, Stefan Knight, Gunter Schneider, Ylva Lindqvist, Tomas Lundqvist & Carl-Ivar Brändén

  2. Central Research and Development Department, E. I. du Pont de Nemours and Co., Wilmington, Delaware, 19898, USA

    George H. Lorimer

Authors
  1. Inger Andersson
    View author publications

    You can also search for this author inPubMed Google Scholar

  2. Stefan Knight
    View author publications

    You can also search for this author inPubMed Google Scholar

  3. Gunter Schneider
    View author publications

    You can also search for this author inPubMed Google Scholar

  4. Ylva Lindqvist
    View author publications

    You can also search for this author inPubMed Google Scholar

  5. Tomas Lundqvist
    View author publications

    You can also search for this author inPubMed Google Scholar

  6. Carl-Ivar Brändén
    View author publications

    You can also search for this author inPubMed Google Scholar

  7. George H. Lorimer
    View author publications

    You can also search for this author inPubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Andersson, I., Knight, S., Schneider, G. et al. Crystal structure of the active site of ribulose-bisphosphate carboxylase. Nature 337, 229–234 (1989). https://doi.org/10.1038/337229a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/337229a0

Search

Advanced 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