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-Structure paper
タイトル | Bacterioferritin nanocage structures uncover the biomineralization process in ferritins. |
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ジャーナル・号・ページ | PNAS Nexus, Vol. 2, Issue 7, Page pgad235, Year 2023 |
掲載日 | 2023年7月20日 |
著者 | Chacko Jobichen / Tan Ying Chong / Rajesh Rattinam / Sandip Basak / Mahalashmi Srinivasan / Yeu Khai Choong / Kannu Priya Pandey / Tran Bich Ngoc / Jian Shi / Jayaraman Angayarkanni / J Sivaraman / |
PubMed 要旨 | 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 ...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 bacterioferritin (ScBfr) nanocage and the subunit crystal structure. The holoforms show different stages of Fe-biomineral accumulation inside the nanocage, in which the connections exist in two of the fourfold channels of the nanocage between the C-terminal of the ScBfr monomers and the Fe-biomineral cluster. The mutation and truncation of the bacterioferritin residues involved in these connections significantly reduced the iron and phosphate binding in comparison with those of the wild type and together explain the underlying mechanism. Collectively, our results represent a prototype for the bacterioferritin nanocage, which reveals insight into its biomineralization and the potential channel for bacterioferritin-associated iron trafficking. |
リンク | PNAS Nexus / PubMed:37529551 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.7 - 5.8 Å |
構造データ | EMDB-33639, PDB-7y6f: EMDB-33640, PDB-7y6g: EMDB-33645, PDB-7y6p: EMDB-36137, PDB-8jax: EMDB-36139, PDB-8jb0: EMDB-36140: Cryo-EM structure of Fe-biomineral from bacterioferritin |
化合物 | ChemComp-FE2: ChemComp-FE: ChemComp-HEM: |
由来 |
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キーワード | METAL BINDING PROTEIN / Bacterioferritin / OXIDOREDUCTASE |