6T00

Crystal structure of Cold Shock Protein B (CSP-B) containing 4-F-Phe modified residues

6T00 の概要

• エントリーDOI: 10.2210/pdb6t00/pdb
• 関連するPDBエントリー: 6SZZ
• 分子名称: Cold shock protein CspD, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: fluorine cold shock protein, structural protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7726.37

構造登録者

Zhou, T.,Mayans, O. (登録日: 2019-10-02, 公開日: 2020-02-26, 最終更新日: 2024-01-24)

主引用文献

Welte, H.,Zhou, T.,Mihajlenko, X.,Mayans, O.,Kovermann, M.
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein.
Sci Rep, 10:2640-2640, 2020

PubMed Abstract: Fluorine labelling represents one promising approach to study proteins in their native environment due to efficient suppressing of background signals. Here, we systematically probe inherent thermodynamic and structural characteristics of the Cold shock protein B from Bacillus subtilis (BsCspB) upon fluorine labelling. A sophisticated combination of fluorescence and NMR experiments has been applied to elucidate potential perturbations due to insertion of fluorine into the protein. We show that single fluorine labelling of phenylalanine or tryptophan residues has neither significant impact on thermodynamic stability nor on folding kinetics compared to wild type BsCspB. Structure determination of fluorinated phenylalanine and tryptophan labelled BsCspB using X-ray crystallography reveals no displacements even for the orientation of fluorinated aromatic side chains in comparison to wild type BsCspB. Hence we propose that single fluorinated phenylalanine and tryptophan residues used for protein labelling may serve as ideal probes to reliably characterize inherent features of proteins that are present in a highly biological context like the cell.

PubMed: 32060391
DOI: 10.1038/s41598-020-59446-w

実験手法

X-RAY DIFFRACTION (2.1 Å)