5KII

PSEUDO T4 LYSOZYME MUTANT - Y88PHE-METHYL

5KII の概要

• エントリーDOI: 10.2210/pdb5kii/pdb
• 関連するPDBエントリー: 5KHZ 5KI1 5KI2 5KI3 5KI8 5KIG 5KIM 5KIO
• 分子名称: Endolysin, 2-HYDROXYETHYL DISULFIDE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: halogen bonds, t4 lysozyme, hydrolase
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19704.49

構造登録者

Scholfield, M.R. (登録日: 2016-06-16, 公開日: 2017-04-12, 最終更新日: 2024-11-13)

主引用文献

Scholfield, M.R.,Ford, M.C.,Carlsson, A.C.,Butta, H.,Mehl, R.A.,Ho, P.S.
Structure-Energy Relationships of Halogen Bonds in Proteins.
Biochemistry, 56:2794-2802, 2017

PubMed Abstract: The structures and stabilities of proteins are defined by a series of weak noncovalent electrostatic, van der Waals, and hydrogen bond (HB) interactions. In this study, we have designed and engineered halogen bonds (XBs) site-specifically to study their structure-energy relationship in a model protein, T4 lysozyme. The evidence for XBs is the displacement of the aromatic side chain toward an oxygen acceptor, at distances that are equal to or less than the sums of their respective van der Waals radii, when the hydroxyl substituent of the wild-type tyrosine is replaced by a halogen. In addition, thermal melting studies show that the iodine XB rescues the stabilization energy from an otherwise destabilizing substitution (at an equivalent noninteracting site), indicating that the interaction is also present in solution. Quantum chemical calculations show that the XB complements an HB at this site and that solvent structure must also be considered in trying to design molecular interactions such as XBs into biological systems. A bromine substitution also shows displacement of the side chain, but the distances and geometries do not indicate formation of an XB. Thus, we have dissected the contributions from various noncovalent interactions of halogens introduced into proteins, to drive the application of XBs, particularly in biomolecular design.

PubMed: 28345933
DOI: 10.1021/acs.biochem.7b00022

実験手法

X-RAY DIFFRACTION (1.56 Å)