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TitleObservation of the Protein-Inorganic Interface of Ferritin by Cryo-Electron Microscopy.
Journal, issue, pagesJ Am Chem Soc, Vol. 147, Issue 4, Page 3333-3340, Year 2025
Publish dateJan 29, 2025
AuthorsSagnik Sen / Amar Thaker / Alison Haymaker / Dewight Williams / Po-Lin Chiu / Brent L Nannenga /
PubMed AbstractVisualizing 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 ...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.
External linksJ Am Chem Soc / PubMed:39815632
MethodsEM (single particle)
Resolution2.1 - 3.3 Å
Structure data

44778

9bpi

EMDB-44778: 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.
PDB-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
Method: EM (single particle) / Resolution: 3.3 Å

44779

9bpj

EMDB-44779: Human light chain ferritin reacted with iron (3 Fe2+ to ferritin monomer ratio). Reconstruction of particles with one nanoparticle.
PDB-9bpj: Human light chain ferritin reacted with iron (3 Fe2+ to ferritin monomer ratio). Reconstruction of particles with one nanoparticle
Method: EM (single particle) / Resolution: 2.85 Å

44780

9bpk

EMDB-44780: Human light chain ferritin reacted with iron (3 Fe2+ to ferritin monomer ratio). Reconstruction of particles with no nanoparticle.
PDB-9bpk: Human light chain ferritin reacted with iron (3 Fe2+ to ferritin monomer ratio). Reconstruction of particles with no nanoparticle
Method: EM (single particle) / Resolution: 2.1 Å

44797

9bq5

EMDB-44797, PDB-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.
Method: EM (single particle) / Resolution: 2.36 Å

Source
  • homo sapiens (human)
KeywordsMETAL BINDING PROTEIN / Iron oxide binding protein

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