Crystal structure of the intensely sweet protein monellin

Craig Ogata, Marcos Hatada, Gail Tomlinson, Whan Chul Shin, Sung Hou Kim

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Abstract

Two unusual proteins, discovered in African berries, possess the interesting property of having a very high specificity for the sweet receptors. These proteins, monellin1,2 and thaumatin3, are approximately 100,000 times sweeter than sugar on a molar basis and several thousand times sweeter on a weight basis. Neither contains carbohydrates or modified amino acids. Several interesting observations have been made about the two proteins: native conformations are important for the sweet taste 4-6, although both proteins are intensely sweet, there are no statistically significant sequence similarities between them7; and despite the absence of sequence similarity, antibodies against thaumatin compete for monellin (as well as many other sweet compounds8,9, but not for chemically modified non-sweet monellin9) and vice versa10. To understand the structural basis of these observations we determined the crystal structure of thaumatin11, and report here the structure of monellin at 3 Å resolution. Monellin consists of two peptide chains, the A chain of 44 residues and the B chain of 50 residues12,13. We find no similarity between the backbone structure of monellin and that of thaumatin.

Original languageEnglish (US)
Pages (from-to)739-742
Number of pages4
JournalNature
Volume328
Issue number6132
StatePublished - Dec 1 1988

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Cite this

Ogata, C., Hatada, M., Tomlinson, G., Shin, W. C., & Kim, S. H. (1988). Crystal structure of the intensely sweet protein monellin. Nature, 328(6132), 739-742.