2F32

Xray crystal structure of lysozyme mutant L20/R63A liganded to ethylguanidinium

2F32 の概要

• エントリーDOI: 10.2210/pdb2f32/pdb
• 関連するPDBエントリー: 2f2q
• 分子名称: Lysozyme, BETA-MERCAPTOETHANOL, N-ETHYLGUANIDINE, ... (4 entities in total)
• 機能のキーワード: molecular switch, t4 lysozyme, nano-bitechnology, protein engineering, protein design, hydrolase
• 由来する生物種: Enterobacteria phage T4
• 細胞内の位置: Host cytoplasm : P00720
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19850.80

構造登録者

Yousef, M.S.,Bischoff, N.,Dyer, C.M.,Baase, W.A.,Matthews, B.W. (登録日: 2005-11-18, 公開日: 2006-04-25, 最終更新日: 2023-08-23)

主引用文献

Yousef, M.S.,Bischoff, N.,Dyer, C.M.,Baase, W.A.,Matthews, B.W.
Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme.
Protein Sci., 15:853-861, 2006

PubMed Abstract: The binding of guanidinium ion has been shown to promote a large-scale translation of a tandemly duplicated helix in an engineered mutant of T4 lysozyme. The guanidinium ion acts as a surrogate for the guanidino group of an arginine side chain. Here we determine whether methyl- and ethylguanidinium provide better mimics. The results show that addition of the hydrophobic moieties to the ligand enhances the binding affinity concomitant with reduction in ligand solubility. Crystallographic analysis confirms that binding of the alternative ligands to the engineered site still drives the large-scale conformational change. Thermal analysis and NMR data show, in comparison to guanidinium, an increase in protein stability and in ligand affinity. This is presumably due to the successive increase in hydrophobicity in going from guanidinium to ethylguanidinium. A fluorescence-based optical method was developed to sense the ligand-triggered helix translation in solution. The results are a first step in the de novo design of a molecular switch that is not related to the normal function of the protein.

PubMed: 16600969
DOI: 10.1110/ps.052020606

実験手法

X-RAY DIFFRACTION (1.8 Å)