ArticlePNAS nexus2023
Bacterioferritin nanocage structures uncover the biomineralization process in ferritins.
Article in PNAS nexus, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Influence of heme and pH on the oligomeric states of Brucella melitensis bacterioferritin.Acta crystallographica. Section D, Structural biology · 2026Article
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- The Mechanism of Mineral Nucleation and Growth in a Mini-Ferritin.Journal of the American Chemical Society · 2025Article
- Design Principles Of Inorganic-Protein Hybrid Materials for Biomedicine.Exploration (Beijing, China) · 2025Review
- Unveiling Structural Heterogeneity and Evolutionary Adaptations of Heteromultimeric Bacterioferritin Nanocages.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Observation of the Assembly of the Nascent Mineral Core at the Nucleation Site of Human Mitochondrial Ferritin.Journal of the American Chemical Society · 2025Article
- A Closer Look at the FeS Heme Bonds in Azotobacter vinelandii Bacterioferritin: QM/MM and Local Mode Analysis.Journal of computational chemistry · 2025Article
- Functional connexion of bacterioferritin in antibiotic production and morphological differentiation in Streptomyces coelicolor.Microbial cell factories · 2024Article
- Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.Acta crystallographica. Section D, Structural biology · 2021Article
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Authors and funding
11 authors.
Funding
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Abstract
Iron is an essential element involved in various metabolic processes. The ferritin family of proteins forms nanocage assembly and is involved in iron oxidation, storage, and mineralization. Although several structures of human ferritins and bacterioferritins have been solved, there is still no complete structure that shows both the trapped Fe-biomineral cluster and the nanocage. Furthermore, whereas the mechanism of iron trafficking has been explained using various approaches, structural details on the biomineralization process (i.e. the formation of the mineral itself) are generally lacking. Here, we report the cryo-electron microscopy (cryo-EM) structures of apoform and biomineral bound form (holoforms) of the
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