PT  - JOURNAL ARTICLE
AU  - Sen, Sagnik
AU  - Thaker, Amar
AU  - Williams, Dewight
AU  - Chiu, Po-Lin
AU  - Nannenga, Brent L.
TI  - Observation of the protein-inorganic interface of ferritin by cryo-electron microscopy
AID  - 10.1101/2024.09.04.611303
DP  - 2024 Jan 01
TA  - bioRxiv
PG  - 2024.09.04.611303
4099  - http://biorxiv.org/content/early/2024/09/04/2024.09.04.611303.short
4100  - http://biorxiv.org/content/early/2024/09/04/2024.09.04.611303.full
AB  - Visualizing the structure of the protein-inorganic interface is critically important for our 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-EM to study the protein-nanoparticle 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 nanoparticle 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.Competing Interest StatementThe authors have declared no competing interest.