7SPV

Crystal structure of photoactive yellow protein (PYP); F92oCNF construct

7SPV の概要

• エントリーDOI: 10.2210/pdb7spv/pdb
• 分子名称: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: photoreceptor, signaling protein
• 由来する生物種: Halorhodospira halophila (Ectothiorhodospira halophila)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14077.74

構造登録者

Weaver, J.B.,Kirsh, J.M.,Boxer, S.G. (登録日: 2021-11-03, 公開日: 2022-05-11, 最終更新日: 2023-11-15)

主引用文献

Weaver, J.B.,Kozuch, J.,Kirsh, J.M.,Boxer, S.G.
Nitrile Infrared Intensities Characterize Electric Fields and Hydrogen Bonding in Protic, Aprotic, and Protein Environments.
J.Am.Chem.Soc., 144:7562-7567, 2022

PubMed Abstract: Nitriles are widely used vibrational probes; however, the interpretation of their IR frequencies is complicated by hydrogen bonding (H-bonding) in protic environments. We report a new vibrational Stark effect (VSE) that correlates the electric field projected on the -C≡N bond to the transition dipole moment and, by extension, the nitrile peak area or integrated intensity. This linear VSE applies to H-bonding and non-H-bonding interactions. It can therefore be generally applied to determine electric fields in all environments. Additionally, it allows for semiempirical extraction of the H-bonding contribution to the blueshift of the nitrile frequency. Nitriles were incorporated at H-bonding and non-H-bonding protein sites using amber suppression, and each nitrile variant was structurally characterized at high resolution. We exploited the combined information available from variations in frequency and integrated intensity and demonstrate that nitriles are a generally useful probe for electric fields.

PubMed: 35467853
DOI: 10.1021/jacs.2c00675

実験手法

X-RAY DIFFRACTION (1.18 Å)