9KP7

Crystal structure of Horse spleen L-ferritin mutant (R59F) with Nile Red

これはPDB形式変換不可エントリーです。

9KP7 の概要

• エントリーDOI: 10.2210/pdb9kp7/pdb
• 分子名称: Ferritin light chain, CADMIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: 24mer cage, phenyl alanine mutant, nile red, metal binding protein
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21331.09

構造登録者

Suzuki, T.,Hishikawa, Y.,Maity, B.,Abe, S.,Ueno, T. (登録日: 2024-11-22, 公開日: 2025-03-05, 最終更新日: 2025-04-30)

主引用文献

Hishikawa, Y.,Suzuki, T.,Maity, B.,Noya, H.,Yoshizawa, M.,Asanuma, A.,Katagiri, Y.,Abe, S.,Nagatoishi, S.,Tsumoto, K.,Ueno, T.
Design of Aromatic Interaction Networks in a Protein Cage Modulated by Fluorescent Ligand Binding.
Adv Sci, 12:e2417030-e2417030, 2025

PubMed Abstract: Dynamic behavior of proteins, such as orientation changes of aromatic residues, plays an important role in controlling biomolecular functions. Protein design that can precisely control such dynamic behavior at the atomic level is a challenging issue. The study reports the development of a system capable of orientational changes of aromatic side chains upon ligand binding. Aromatic pockets are constructed on the inner surfaces of protein cages to bind polycyclic aromatic fluorescent molecules to the targeted position by π-π stacking interactions. X-ray crystal structural analysis indicated the cooperative orientation changes of the aromatic clusters around the pocket triggered by the ligand binding. A comparison of various ligands shows that the movement of aromatic clusters can be controlled depending on the ligand structures. Fluorescence quantum yield and fluorescence lifetime are enhanced due to isolation of the fluorescent molecules in an aromatic pocket. These findings provide an understanding of the unique molecular behavior and fluorescence properties of ligands due to the assembly of aromatic residues and a guideline for developing dynamically controlled supramolecular biomaterials.

PubMed: 39973762
DOI: 10.1002/advs.202417030

実験手法

X-RAY DIFFRACTION (1.5 Å)