Structural highlights
Publication Abstract from PubMed
Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27A. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Calpha atom of G96 in thaumatin II was observed. Furthermore, the side chain of residue 67 in thaumatin II is highly disordered. Since residue 67 is one of two residues critical to the sweetness of thaumatin, the present results suggested that the critical positive charges at positions 67 and 82 are disordered and the flexibility and fluctuation of these side chains would be suitable for interaction of thaumatin molecules with sweet receptors.
Crystal structure of the sweet-tasting protein thaumatin II at 1.27A.,Masuda T, Ohta K, Tani F, Mikami B, Kitabatake N Biochem Biophys Res Commun. 2011 Jul 8;410(3):457-60. Epub 2011 Jun 6. PMID:21672520[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Masuda T, Ohta K, Tani F, Mikami B, Kitabatake N. Crystal structure of the sweet-tasting protein thaumatin II at 1.27A. Biochem Biophys Res Commun. 2011 Jul 8;410(3):457-60. Epub 2011 Jun 6. PMID:21672520 doi:10.1016/j.bbrc.2011.05.158
