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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.

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Author notes

  1. Clive Little: Deceased.

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
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  2. Lars Kristian Hansen
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  3. Bjørn Birknes
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  4. Knut Jynge
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  5. Sissel Hansen
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  6. Asbjørn Hordvik
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  7. Clive Little
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  8. Eleanor Dodson
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  9. Zygmunt Derewenda
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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

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