9KF5
Crystal structure of Ferritin mutant(E53H/E57H)
Summary for 9KF5
| Entry DOI | 10.2210/pdb9kf5/pdb |
| Descriptor | Ferritin light chain, 1,2-ETHANEDIOL, CADMIUM ION, ... (6 entities in total) |
| Functional Keywords | 24-mer ferritin cage histidine mutant, metal binding protein |
| Biological source | Equus caballus (horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 20820.61 |
| Authors | |
| Primary citation | 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:-, 2025 Cited by 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: 40272036DOI: 10.1002/anie.202504608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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