ArticleThe Journal of biological chemistry2013
The role of nonconserved residues of Archaeoglobus fulgidus ferritin on its unique structure and biophysical properties.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 56 citations in OpenAlex.
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- Molecular Mechanisms and Biomedical Applications of Ferritin Nanocages: A Comprehensive Review of Self-Assembly, Engineering, and Multifunctional Delivery Platforms.International journal of nanomedicine · 2026Review
- Cellular Uptake of Phase-Separating Peptide Coacervates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Ferritin cages as building blocks for higher-order assembly through copper-sulfur bonds for HER analysis.RSC advances · 2024Article
- Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024Article
- Structural and Functional Insights into the Roles of Potential Metal-Binding Sites inPolymers · 2022Article
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- Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates.Pharmaceutics · 2021Article
- Polyelectrolyte Encapsulation and Confinement within Protein Cage-Inspired Nanocompartments.Pharmaceutics · 2021Review
- Self-assembling ferritin-dendrimer nanoparticles for targeted delivery of nucleic acids to myeloid leukemia cells.Journal of nanobiotechnology · 2021Article
- Ferritin Nanocages for Protein Delivery to Tumor Cells.Molecules (Basel, Switzerland) · 2020Review
- Ferritin nanovehicle for targeted delivery of cytochrome C to cancer cells.Scientific reports · 2019Article
- Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering.Biophysical reviews · 2019Review
- Magnetoferritin: Process, Prospects, and Their Biomedical Applications.International journal of molecular sciences · 2019Review
- Protein cage assembly across multiple length scales.Chemical Society reviews · 2018Review
- Excimer based fluorescent pyrene-ferritin conjugate for protein oligomerization studies and imaging in living cells.RSC advances · 2018Article
- Thermostable exoshells fold and stabilize recombinant proteins.Nature communications · 2017Article
- Structural-functional analysis of engineered protein-nanoparticle assemblies using graphene microelectrodes.Chemical science · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Archaeoglobus fulgidus ferritin (AfFtn) is the only tetracosameric ferritin known to form a tetrahedral cage, a structure that remains unique in structural biology. As a result of the tetrahedral (2-3) symmetry, four openings (∼45 Å in diameter) are formed in the cage. This open tetrahedral assembly contradicts the paradigm of a typical ferritin cage: a closed assembly having octahedral (4-3-2) symmetry. To investigate the molecular mechanism affecting this atypical assembly, amino acid residues Lys-150 and Arg-151 were replaced by alanine. The data presented here shed light on the role that these residues play in shaping the unique structural features and biophysical properties of the AfFtn. The x-ray crystal structure of the K150A/R151A mutant, solved at 2.1 Å resolution, indicates that replacement of these key residues flips a "symmetry switch." The engineered molecule no longer assembles with tetrahedral symmetry but forms a typical closed octahedral ferritin cage. Small angle x-ray scattering reveals that the overall shape and size of AfFtn and AfFtn-AA in solution are consistent with those observed in their respective crystal structures. Iron binding and release kinetics of the AfFtn and AfFtn-AA were investigated to assess the contribution of cage openings to the kinetics of iron oxidation, mineralization, or reductive iron release. Identical iron binding kinetics for AfFtn and AfFtn-AA suggest that Fe(2+) ions do not utilize the triangular pores for access to the catalytic site. In contrast, relatively slow reductive iron release was observed for the closed AfFtn-AA, demonstrating involvement of the large pores in the pathway for iron release.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.