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Mini-Bacterioferritin: New Ferritin Family Member Discovered in Methane-Oxidizing Archaeon
Researchers have identified a novel member of the ferritin family, dubbed mini-bacterioferritin, from the methanotrophic archaeon 'Candidatus Methanoperedens carboxydivorans'. The protein's structure reveals a 12-mer assembly and distinctive characteristics previously found only in 24-mer bacterioferritins, suggesting it may conserve ancestral traits.
A new member of the ferritin family of proteins has been discovered and dubbed mini-bacterioferritin. Ferritins are found in nearly all life forms and are critical for iron homeostasis. The mini-bacterioferritin was isolated from a microbial enrichment dominated by the methanotrophic archaeon 'Candidatus Methanoperedens carboxydivorans'. According to the study in *Communications Biology*, the protein's atomic resolution crystal structure shows a 12-mer assembly with a diiron ferroxidase centre located within a four-helix bundle. Redox-cycling experiments on protein crystals show a shift in iron position at the active site, following the established ferritin catalytic cycle. The 12-mer sphere-like structure also contains six Fe-coproporphyrin III ligands, positioned at the interdimeric interface. This characteristic was previously only found in 24-mer bacterioferritins.
Key Facts
- Mini-bacterioferritin, a novel member of the ferritin family, has been identified.
- The mini-bacterioferritin was isolated from the methanotrophic archaeon 'Candidatus Methanoperedens carboxydivorans'.
- The protein structure reveals a 12-mer assembly with a diiron ferroxidase centre.
- Redox-cycling experiments show a shift in iron position at the active site.
- The structure contains six Fe-coproporphyrin III ligands at the interdimeric interface.
- This characteristic was previously only found in 24-mer bacterioferritins.
- Mini-bacterioferritins form a distinct clade within the ferritin family that might conserve ancestral traits.
- Future research is needed to investigate the physiological roles of these enzymes.