3AOK

Crystal structure of sweet-tasting protein thaumatin II

3AOK の概要

• エントリーDOI: 10.2210/pdb3aok/pdb
• 関連するPDBエントリー: 3AL7 3ALD
• 分子名称: Thaumatin-2, L(+)-TARTARIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: thaumatin family, mainly beta, taste protein, sweet receptor, aril, plant protein
• 由来する生物種: Thaumatococcus daniellii
• 細胞内の位置: Cytoplasmic vesicle: P02884
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22980.74

構造登録者

Masuda, T.,Mikami, B.,Kitabatake, N. (登録日: 2010-10-01, 公開日: 2011-07-27, 最終更新日: 2024-10-16)

主引用文献

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

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: 21672520
DOI: 10.1016/j.bbrc.2011.05.158

実験手法

X-RAY DIFFRACTION (1.27 Å)