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