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.

  • Letter
  • Published:

High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus

Nature volume 338, pages 357–360 (1989)Cite this article

Abstract

BOTH the phosphatidylinositol-hydrolysing and the phos-phatidylcholine-hydrolysing phospholipases C have been implicated in the generation of second messengers in mammalian cells1,2. The phosphatidylcholine-hydrolysing phospholipase C(PLC) from Bacillus cereus, a monomeric protein containing 245 amino-acid residues3, is similar to some of the corresponding mammalian proteins4. This, together with the fact that the bacterial enzyme can mimic the action of mammalian PLC in causing, for example, enhanced prostaglandin biosynthesis5, suggests that B. cereus PLC can be used as a model for the hitherto poorly characterized mammalian PLCs. We report here the three-dimensional structure of B. cereus PLC at 1.5 Å resolution. The enzyme is an all-helix protein belonging to a novel structural class and contains, at least in the crystalline state, three Zn2+ in the active site. We also present preliminary results from a study at 1.9 Å resolution of the complex between PLC and inorganic phosphate (Pi) which indicate that the substrate binds directly to the metal ions.

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

Access options

Buy this article

  • Purchase on Springer Link
  • 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. Berridge, M. J. Biochem. J. 220, 345–360 (1984).

    Article  CAS  Google Scholar 

  2. Besterman, J. M., Duronio, V. & Cuatracosa, P. Proc. natn. Acad. Sci. U.S.A. 83, 6785–6789 (1986).

    Article  CAS  ADS  Google Scholar 

  3. Johansen, T. et al. Gene 65, 293–304 (1988).

    Article  CAS  Google Scholar 

  4. Clark, M. A., Shorr, R. G. L. & Bomalski, J. S. Biochem. biophys. Res. Commun. 140, 114–119 (1986).

    Article  CAS  Google Scholar 

  5. Levine, L. Xiao, D.-M. & Little, C. Prostaglandins 34, 633–642 (1988).

    Article  Google Scholar 

  6. Wang, B. C. Meth. Enzym. 115, 90–112 (1985).

    Article  CAS  Google Scholar 

  7. Keith, C. et al. J. molec. Biol. 256, 8602–8607 (1981).

    CAS  Google Scholar 

  8. Dijkstra, B. W., Kalk, K. H., Hol, W. G. J. & Drenth, J. J. molec. Biol. 147, 97–123 (1981).

    Article  CAS  Google Scholar 

  9. Dijkstra, B. W., Renetseder, R., Kalk, K. H., Hol, W. G. J. & Drenth, J. J. molec. Biol. 168, 163–179 (1981).

    Article  Google Scholar 

  10. Brunie, S., Bolin, J., Gewirth, D. & Sigler, P. B. J. biol. Chem. 260, 9,742–9,749 (1985).

    CAS  Google Scholar 

  11. Aalmo, K. et al. Biochem. Internatn. 8, 27–33 (1984).

    CAS  Google Scholar 

  12. Little, C. & Otnaess, A.-B. Bochim. biophys. Acta 391, 326–333 (1975).

    Article  CAS  Google Scholar 

  13. Little, C. & Johansen, S. Biochem J. 179, 509–514 (1979).

    Article  CAS  Google Scholar 

  14. Sowadski, J. M., Handschumaker, M. D., Krishna Murthy, H. M., Foster, B. A. & Wyckoff, H. W. J. molec. Biol. 186, 417–433 (1985).

    Article  CAS  Google Scholar 

  15. Ollis, D. L., Brick, P., Hamlin, R., Xuong, N. G. & Steltz, T. A. Nature 313, 762–766 (1985).

    Article  CAS  ADS  Google Scholar 

  16. Joyce, C. M. & Steitz, T. A. Trends biochem. Sci. 12, 288–292 (1987).

    Article  CAS  Google Scholar 

  17. Suck, D. & Oefner, C. Nature 321, 620–625 (1986).

    Article  CAS  ADS  Google Scholar 

  18. Renetseder, R., Brunie, S., Dijkstra, B. W., Drenth, J. & Sigler, P. B. J. biol. Chem. 260, 11,627–11,634 (1985).

    CAS  Google Scholar 

  19. Little, C. Acta chem. scand. B35, 39–44 (1981).

    Article  CAS  Google Scholar 

  20. Dayne, T. & Pepinsky, R. Acta crystallogr. 10, 438–439 (1957).

    Article  Google Scholar 

  21. Grammacioli, C. M. Acta crystallogr. 21, 600–605 (1966).

    Article  Google Scholar 

  22. Coleman, J. E. & Gettins, P. Adv. Enzymol. 55, 821–862 (1983).

    Google Scholar 

  23. Sherriff, S., Hendrickson, W. A. & Smith, J. L. J. molec. Biol. 197, 273–296 (1987).

    Article  Google Scholar 

  24. Rees, D. C., Lewis, M. & Lipscomb, W. N. J. molec. Biol. 168, 367–387 (1983).

    Article  CAS  Google Scholar 

  25. Bicknell, R., Hanson, G. R., Holmquist, B. & Little, C. Biochemistry 25, 4,219–4,233 (1986).

    Article  CAS  Google Scholar 

  26. Feiters, M. C., Little, C. & Waley, S. G. J. Phys., Paris 47, 1169–1,172 (1986).

    Google Scholar 

  27. Otnaess, A. B., Prydz, H., Bjørkelid, E. & Berre, Å. Eur. J. Biochem. 27, 238–243 (1972).

    Article  CAS  Google Scholar 

  28. Little, C. Biochem. J. 175, 977–986 (1978).

    Article  CAS  Google Scholar 

  29. Holmes, M. A. & Matthews, B. W. J. molec. Biol. 160, 623–639 (1982).

    Article  CAS  Google Scholar 

  30. Murthy, M. R. N., Reid, T. J., Sicignano, A., Tanaka, N. & Rossman, M. G. J. molec. Biol. 152, 465–499 (1981).

    Article  CAS  Google Scholar 

  31. Vainshtein, B. K. et al. J. molec. Biol. 188, 49–61 (1986).

    Article  CAS  Google Scholar 

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

    Article  CAS  ADS  Google Scholar 

  33. Hough, E., Little, C. & Jynge, K. J. molec. Biol. 121, 567–570 (1987).

    Article  Google Scholar 

  34. Helliwell, J. R. et al. Nucl. Instrum. Meth. A246, 617–623 (1986).

    Article  CAS  ADS  Google Scholar 

  35. Hendrickson, W. A. Meth. Enzym. 115, 252–270 (1985).

    Article  CAS  Google Scholar 

  36. Luzzati, V. Acta crystallogr. 5, 802–810 (1952).

    Article  Google Scholar 

  37. Vijayan, M. in Structural Studies on Molecules of Biological Interest (eds Dodson, G., Glusker, J. P. & Sayre, D.) 260–273 Clarendon, Oxford, 1981).

    Google Scholar 

  38. Titball, R. W. et al. Infect. Immunity 57, 367–376 (1989).

    CAS  Google Scholar 

  39. Yun Tso, J. & Siebel, C. Infect. Immunity 57, 468–476 (1989).

    Google Scholar 

  40. Leslie, D., Fairweather, N., Pickard, D., Dougan, G. & Kehoe, M. J. molec. Microbiol. (in the press).

  41. Remington, S., Wiegand, G. & Huber, R. J. molec. Biol. 158, 111–152 (1982).

    Article  CAS  Google Scholar 

Download references

Author information

Author notes

  1. Clive Little: Deceased.

Authors and Affiliations

  1. Protein Crystallography Group, Department of Chemistry, University of Tromsø, Box 953, N-9001, Tromsø, Norway

    Edward Hough, Lars Kristian Hansen, Bjørn Birknes, Knut Jynge, Sissel Hansen & Asbjørn Hordvik

  2. Institute of Medical Biology, University of Tromsø, Box 977, N-9001, Tromsø, Norway

    Clive Little

  3. Department of Chemistry, University of York, Heslington, York, Y01 5DD, UK

    Eleanor Dodson & Zygmunt Derewenda

Authors
  1. Edward Hough
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Lars Kristian Hansen
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Bjørn Birknes
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Knut Jynge
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Sissel Hansen
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Asbjørn Hordvik
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Clive Little
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. Eleanor Dodson
    View author publications

    You can also search for this author in PubMed Google Scholar

  9. Zygmunt Derewenda
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hough, E., Hansen, L., Birknes, B. et al. High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus. Nature 338, 357–360 (1989). https://doi.org/10.1038/338357a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/338357a0

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

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