8P2Q

Crystal structure of Hen Egg White Lysozyme co-crystallized with 10 mM TbXo4-OH

8P2Q の概要

• エントリーDOI: 10.2210/pdb8p2q/pdb
• 関連するPDBエントリー: 8OWC
• 分子名称: Lysozyme C, TbXo4-OH, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: hewl, crystallophore variants, nucleating agent, hydrolase
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17072.35

構造登録者

Alsalman, Z.,Girard, E. (登録日: 2023-05-16, 公開日: 2024-06-05, 最終更新日: 2024-11-20)

主引用文献

Roux, A.,Alsalman, Z.,Jiang, T.,Mulatier, J.C.,Pitrat, D.,Dumont, E.,Riobe, F.,Gillet, N.,Girard, E.,Maury, O.
Influence of Chemical Modifications of the Crystallophore on Protein Nucleating Properties and Supramolecular Interactions Network.
Chemistry, 30:e202400900-e202400900, 2024

PubMed Abstract: Crystallophores are lanthanide complexes that have demonstrated outstanding induction of crystallization for various proteins. This article explores the effect of tailored modifications of the crystallophore first generation and their impact on the nucleating properties and protein crystal structures. Through high-throughput crystallization experiments and dataset analysis, we evaluated the effectiveness of these variants, in comparison to the first crystallophore generation G. In particular, the V variant, featuring a propanol pendant arm, demonstrated the ability to produce new crystallization conditions for the proteins tested (hen-egg white lysozyme, proteinase K and thaumatin). Structural analysis performed in the case of hen egg-white lysozyme along with Molecular Dynamics simulations, highlights V's unique behavior, taking advantage of the flexibility of its propanol arm to explore different protein surfaces and form versatile supramolecular interactions.

PubMed: 38738452
DOI: 10.1002/chem.202400900

実験手法

X-RAY DIFFRACTION (1.69 Å)