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.
Original language | English (US) |
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Pages (from-to) | 427-431 |
Number of pages | 5 |
Journal | Nature Structural Biology |
Volume | 5 |
Issue number | 6 |
DOIs | |
State | Published - 1998 |