9KF7

Crystal structure of ferritin mutant (R52H/E56H/R59H/E63H)

9KF7 の概要

• エントリーDOI: 10.2210/pdb9kf7/pdb
• 分子名称: Ferritin light chain, 1,2-ETHANEDIOL, CADMIUM ION, ... (6 entities in total)
• 機能のキーワード: 24-mer ferritin cage histidine mutant, 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: 20974.64

構造登録者

Tian, J.,Maity, B.,Furuta, T.,Pan, T.,Abe, S.,Ueno, T. (登録日: 2024-11-05, 公開日: 2025-09-24, 最終更新日: 2025-10-08)

主引用文献

Tian, J.,Maity, B.,Furuta, T.,Pan, T.,Ueno, T.
An Artificial Metal-Free Peroxidase Designed Using a Ferritin Cage for Bioinspired Catalysis.
Angew.Chem.Int.Ed.Engl., 64:e202504608-e202504608, 2025

PubMed Abstract: Developing artificial enzymes is challenging because it requires precise design of active sites with well-arranged amino acid residues. Histidine-rich oligopeptides have been recently shown to exhibit peroxidase-mimetic activities, but their catalytic function relies on maintaining unique supramolecular structures. This work demonstrates the design of a specific array of histidine residues on the internal surface of the ferritin cage to function as an active center for catalysis. The crystal structures of the ferritin mutants revealed histidine-histidine interactions, forming well-defined histidine clusters (His-clusters). These mutants exhibit peroxidase-mimetic activities by oxidizing 3,3',5,5'-tetramethylbenzidine (TMB) in the presence of hydrogen peroxide. Molecular dynamics simulations further highlight the co-localization of TMB and hydrogen peroxide at the histidine-rich clusters, indicating that the confined environment of the ferritin cage enhances their interactions. This study presents a simple yet effective approach to design metal-free artificial enzymes, paving the way for innovations in bioinspired catalysis.

PubMed: 40272036
DOI: 10.1002/anie.202504608

実験手法

X-RAY DIFFRACTION (1.5 Å)