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Solution structure of the thermostable sweet-tasting protein brazzein

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Abstract

The fruit of Pentadiplandra brazzeana Baillon contains a small, sweet-tasting protein named brazzein. The structure of brazzein in solution was determined by proton nuclear magnetic resonance spectroscopy at pH 5.2 and 22 °C. The brazzein fold, which contains one α-helix and three strands of antiparallel β-sheet, does not resemble that of either of the other two sweet-tasting proteins with known structures, monellin and thaumatin. Instead, the structure of brazzein resembles those of plant γ-thionins and defensins and arthropod toxins. Sequence comparisons predict that members of a newly-identified family of serine proteinase inhibitors share the brazzein fold.

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Author information

Author notes

  1. Jane E. Caldwell

    Present address: Division of Hematology and Oncology, New England Medical Center, 750 Washington Street, Boston, Massachusetts, 02111, USA

  2. Ding Ming

    Present address: Ingredient and Flavor Technology, Pepsi-Cola Company, Valhalla, New York, 10595, USA

Authors and Affiliations

  1. Graduate Program in Biophysics, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA

    Jane E. Caldwell & John L. Markley

  2. Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA

    Frits Abildgaard, Željko Džakula & John L. Markley

  3. National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA

    Frits Abildgaard, Željko Džakula & John L. Markley

  4. Department of Animal Health and Biomedical Sciences, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA

    Ding Ming & Göran Hellekant

Authors
  1. Jane E. Caldwell
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  2. Frits Abildgaard
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  3. Željko Džakula
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  4. Ding Ming
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  5. Göran Hellekant
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  6. John L. Markley
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Corresponding author

Correspondence to John L. Markley.

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Caldwell, J., Abildgaard, F., Džakula, Ž. et al. Solution structure of the thermostable sweet-tasting protein brazzein. Nat Struct Mol Biol 5, 427–431 (1998). https://doi.org/10.1038/nsb0698-427

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  • DOI: https://doi.org/10.1038/nsb0698-427

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