3WOU

Crystal Structure of The Recombinant Thaumatin II at 0.99 A

3WOU の概要

• エントリーDOI: 10.2210/pdb3wou/pdb
• 関連するPDBエントリー: 3WOX 3al7 3ald 3aok 3vhf 3vhg 3vjq
• 分子名称: Thaumatin-2, L(+)-TARTARIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: osmotin, thaumatin-like protein, sweet-tasting protein, sweet receptors, plant protein
• 由来する生物種: Thaumatococcus daniellii (katemfe)
• 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: 22796.55

構造登録者

Masuda, T.,Mikami, B.,Tani, F. (登録日: 2013-12-30, 公開日: 2014-10-22, 最終更新日: 2024-11-06)

主引用文献

Masuda, T.,Mikami, B.,Tani, F.
Atomic structure of recombinant thaumatin II reveals flexible conformations in two residues critical for sweetness and three consecutive glycine residues
Biochimie, 106:33-38, 2014

PubMed Abstract: Thaumatin, an intensely sweet-tasting protein used as a sweetener, elicits a sweet taste at 50 nM. Although two major variants designated thaumatin I and thaumatin II exist in plants, there have been few dedicated thaumatin II structural studies and, to date, data beyond atomic resolution had not been obtained. To identify the detailed structural properties explaining why thaumatin elicits a sweet taste, the structure of recombinant thaumatin II was determined at the resolution of 0.99 Å. Atomic resolution structural analysis with riding hydrogen atoms illustrated the differences in the direction of the side-chains more precisely and the electron density maps of the C-terminal regions were markedly improved. Though it had been suggested that the three consecutive glycine residues (G142-G143-G144) have highly flexible conformations, G143, the central glycine residue was successfully modelled in two conformations for the first time. Furthermore, the side chain r.m.s.d. values for two residues (R67 and R82) critical for sweetness exhibited substantially higher values, suggesting that these residues are highly disordered. These results demonstrated that the flexible conformations in two critical residues favoring their interaction with sweet taste receptors are prominent features of the intensely sweet taste of thaumatin.

PubMed: 25066915
DOI: 10.1016/j.biochi.2014.07.016

実験手法

X-RAY DIFFRACTION (0.99 Å)