3AOK
Crystal structure of sweet-tasting protein thaumatin II
Summary for 3AOK
| Entry DOI | 10.2210/pdb3aok/pdb |
| Related | 3AL7 3ALD |
| Descriptor | Thaumatin-2, L(+)-TARTARIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | thaumatin family, mainly beta, taste protein, sweet receptor, aril, plant protein |
| Biological source | Thaumatococcus daniellii |
| Cellular location | Cytoplasmic vesicle: P02884 |
| Total number of polymer chains | 1 |
| Total formula weight | 22980.74 |
| Authors | Masuda, T.,Mikami, B.,Kitabatake, N. (deposition date: 2010-10-01, release date: 2011-07-27, Last modification date: 2024-10-16) |
| Primary citation | 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., 410:457-460, 2011 Cited by PubMed Abstract: Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50 nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27 Å. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Cα 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. PubMed: 21672520DOI: 10.1016/j.bbrc.2011.05.158 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.27 Å) |
Structure validation
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