ArticleFEBS open bio2021
Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta.
Article in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Molecular Mechanisms and Biomedical Applications of Ferritin Nanocages: A Comprehensive Review of Self-Assembly, Engineering, and Multifunctional Delivery Platforms.International journal of nanomedicine · 2026Review
- Bioactive Ingredients, Functions, and Development Strategies ofFood science & nutrition · 2025Review
- Article
- Structural and Functional Insights into the Roles of Potential Metal-Binding Sites inPolymers · 2022Article
- Crystallographic characterization of a marine invertebrate ferritin from the sea cucumber Apostichopus japonicus.FEBS open bio · 2022Article
- Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood ClamFrontiers in molecular biosciences · 2022Article
- Conservative and Atypical Ferritins of Sponges.International journal of molecular sciences · 2021Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For marine invertebrates with no adaptive immune system, ferritin is a major intracellular iron-storage protein with a critical role in innate immunity. Here, we present the crystal structures of two novel ferritins [Fer147 and Phascolosoma esculenta ferritin (PeFer)] from the marine invertebrate P. esculenta, which resides in muddy-bottom coastal regions. Fer147 and PeFer exhibit the 4-3-2 symmetry of cage-like hollow shells containing 24 subunits, similar to other known ferritins. Fer147 and PeFer contain both the conserved ferroxidase center and threefold channels. Subtle structural differences in the putative nucleation sites suggest possible routes of metal ion movement in the protein shells. However, the marked variation in the electrostatic potential of the threefold channels in Fer147 and the fourfold channels in PeFer suggests significant diversity between Fer147 and PeFer in terms of metal ion aggregation and cation exclusion. In summary, the presented crystal structures may serve as references for studies of the iron-storage mechanism of additional ferritins from marine invertebrates.
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