4he7
Crystal Structure of Brazzein
Structural highlights
FunctionDEF_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 PubMedBrazzein is the smallest sweet-tasting protein and was isolated from the wild African plant Pentadiplandra brazzeana. The brazzein molecule consists of 54 amino-acid residues and four disulfide bonds. Here, the first crystal structure of brazzein is reported at 1.8 A resolution and is compared with previously reported solution structures. Despite the overall structural similarity, there are several remarkable differences between the crystal and solution structures both in their backbone folds and side-chain conformations. Firstly, there is an additional alpha-helix in the crystal structure. Secondly, the atomic r.m.s.d.s between the corresponding C(alpha)-atom pairs are as large as 2.0-2.2 A between the crystal and solution structures. Thirdly, the crystal structure exhibits a molecular shape that is similar but not identical to the solution structures. The crystal structure of brazzein reported here will provide additional information and further insights into the intermolecular interaction of brazzein with the sweet-taste receptor. The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana.,Nagata K, Hongo N, Kameda Y, Yamamura A, Sasaki H, Lee WC, Ishikawa K, Suzuki E, Tanokura M Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):642-7. doi:, 10.1107/S0907444913001005. Epub 2013 Mar 14. PMID:23519673[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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