5LC7

Crystal structure of a single chain monellin mutant: E23Q/Q28K/C41S/Y65R-MNEI

5LC7 の概要

• エントリーDOI: 10.2210/pdb5lc7/pdb
• 分子名称: Monellin chain B,Monellin chain A (2 entities in total)
• 機能のキーワード: plant protein, sweet protein
• 由来する生物種: Dioscoreophyllum cumminsii (Serendipity berry); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22794.14

構造登録者

Pica, A.,Merlino, A. (登録日: 2016-06-19, 公開日: 2016-10-05, 最終更新日: 2024-01-10)

主引用文献

Leone, S.,Pica, A.,Merlino, A.,Sannino, F.,Temussi, P.A.,Picone, D.
Sweeter and stronger: enhancing sweetness and stability of the single chain monellin MNEI through molecular design.
Sci Rep, 6:34045-34045, 2016

PubMed Abstract: Sweet proteins are a family of proteins with no structure or sequence homology, able to elicit a sweet sensation in humans through their interaction with the dimeric T1R2-T1R3 sweet receptor. In particular, monellin and its single chain derivative (MNEI) are among the sweetest proteins known to men. Starting from a careful analysis of the surface electrostatic potentials, we have designed new mutants of MNEI with enhanced sweetness. Then, we have included in the most promising variant the stabilising mutation E23Q, obtaining a construct with enhanced performances, which combines extreme sweetness to high, pH-independent, thermal stability. The resulting mutant, with a sweetness threshold of only 0.28 mg/L (25 nM) is the strongest sweetener known to date. All the new proteins have been produced and purified and the structures of the most powerful mutants have been solved by X-ray crystallography. Docking studies have then confirmed the rationale of their interaction with the human sweet receptor, hinting at a previously unpredicted role of plasticity in said interaction.

PubMed: 27658853
DOI: 10.1038/srep34045

実験手法

X-RAY DIFFRACTION (1.55 Å)