Publication Abstract from PubMed
Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at a concentration of 50 nM. The crystal structure of a recombinant form of thaumatin I produced in the yeast Pichia pastoris has been determined to a resolution of 1.1 A. The model was refined with anisotropic B parameters and riding H atoms. A comparison of the diffraction data and refinement statistics for recombinant thaumatin I with those for plant thaumatin I revealed no significant differences in the diffraction data. The R values for recombinant thaumatin I and plant thaumatin I (F(o) > 4sigma) were 9.11% and 9.91%, respectively, indicating the final model to be of good quality. Notably, the electron-density maps around Asn46 and Ser63, which differ between thaumatin variants, were significantly improved. Furthermore, a number of H atoms became visible in an OMIT map and could be assigned. The high-quality structure of recombinant thaumatin with H atoms should provide details about sweetness determinants in thaumatin and provide valuable insights into the mechanism of its interaction with taste receptors.
High-resolution structure of the recombinant sweet-tasting protein thaumatin I.,Masuda T, Ohta K, Mikami B, Kitabatake N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jun 1;67(Pt, 6):652-8. Epub 2011 May 24. PMID:21636903[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
