9BQ5
C-terminus truncated (last two residues) mutant of Human light chain ferritin reacted with iron (3 Fe2+ to ferritin monomer ratio). Reconstruction of particles with no nanoparticle.
Summary for 9BQ5
| Entry DOI | 10.2210/pdb9bq5/pdb |
| Related | 9BPI 9BPJ 9BPK |
| EMDB information | 44797 |
| Descriptor | Ferritin light chain (1 entity in total) |
| Functional Keywords | iron oxide binding protein, metal binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 24 |
| Total formula weight | 471942.00 |
| Authors | |
| Primary citation | Sen, S.,Thaker, A.,Haymaker, A.,Williams, D.,Chiu, P.L.,Nannenga, B.L. Observation of the Protein-Inorganic Interface of Ferritin by Cryo-Electron Microscopy. J.Am.Chem.Soc., 147:3333-3340, 2025 Cited by PubMed Abstract: Visualizing the structure of the protein-inorganic interface is critically important for a more complete understanding of biomineralization. Unfortunately, there are limited approaches for the direct and detailed study of biomolecules that interact with inorganic materials. Here, we use single-particle cryo-electron microscopy (cryo-EM) to study the protein-nanoparticle (NP) interactions of human light chain ferritin and visualize the high-resolution details of the protein-inorganic interface. In this work, we determined the 2.85 Å structure of human light chain ferritin bound to its native iron oxide NP substrate. The resulting cryo-EM maps confirmed and enhanced previously proposed interactions of the protein with the material along the B-helix and revealed new interaction at the C-terminus of light chain ferritin. This work sheds new light on the mechanisms of ferritin biomineralization and further demonstrates the application of cryo-EM for the study of protein-inorganic systems. PubMed: 39815632DOI: 10.1021/jacs.4c13873 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.36 Å) |
Structure validation
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