Structural highlights
Function
[DEF_PENBA] Taste-modifying protein; sweet-tasting. It is 2000 sweeter than sucrose on a molar basis.[1] Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.[2]
Publication Abstract from PubMed
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 degrees C. The brazzein fold, which contains one alpha-helix and three strands of antiparallel beta-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 gamma-thionins and defensins and arthropod toxins. Sequence comparisons predict that members of a newly-identified family of serine proteinase inhibitors share the brazzein fold.
Solution structure of the thermostable sweet-tasting protein brazzein.,Caldwell JE, Abildgaard F, Dzakula Z, Ming D, Hellekant G, Markley JL Nat Struct Biol. 1998 Jun;5(6):427-31. PMID:9628478[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yount NY, Yeaman MR. Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. Epub 2004 Apr 26. PMID:15118082 doi:10.1073/pnas.0401567101
- ↑ Yount NY, Yeaman MR. Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. Epub 2004 Apr 26. PMID:15118082 doi:10.1073/pnas.0401567101
- ↑ Caldwell JE, Abildgaard F, Dzakula Z, Ming D, Hellekant G, Markley JL. Solution structure of the thermostable sweet-tasting protein brazzein. Nat Struct Biol. 1998 Jun;5(6):427-31. PMID:9628478
