9BPI

C-terminus truncated (last two residues) mutant of Human light chain ferritin reacted with Ferrous salt(3 Fe2+ per ferritin subunit) . Reconstruction of particles with one nanoparticle

Summary for 9BPI

• Entry DOI: 10.2210/pdb9bpi/pdb
• Related: 9BPJ 9BPK
• EMDB information: 44778
• 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: 478019.66

Authors

Sen, S.,Nannenga, B.L.,Williams, D. (deposition date: 2024-05-07, release date: 2025-05-14)

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

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: 39815632
DOI: 10.1021/jacs.4c13873

Experimental method

ELECTRON MICROSCOPY (3.3 Å)