Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Bacterioferritin nanocage structures uncover the biomineralization process in ferritins.
Journal, issue, pages	PNAS Nexus, Vol. 2, Issue 7, Page pgad235, Year 2023
Publish date	Jul 20, 2023
Authors	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 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 ...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.
External links	PNAS Nexus / PubMed:37529551 / PubMed Central
Methods	EM (single particle)
Resolution	2.7 - 5.8 Å
Structure data	33639 7y6f EMDB-33639, PDB-7y6f: Cryo-EM structure of Apo form of ScBfr Method: EM (single particle) / Resolution: 2.7 Å 33640 7y6g EMDB-33640, PDB-7y6g: Cryo-EM structure of bacterioferritin holoform 1a Method: EM (single particle) / Resolution: 3.6 Å 33645 7y6p EMDB-33645, PDB-7y6p: Cryo-EM structure if bacterioferritin holoform Method: EM (single particle) / Resolution: 3.3 Å 36137 8jax EMDB-36137, PDB-8jax: Cryo-EM structure of Holo form of ScBfr with O symmetry Method: EM (single particle) / Resolution: 3.27 Å 36139 8jb0 EMDB-36139, PDB-8jb0: Cryo-EM structure of Holo form of ScBfr in C1 symmetry Method: EM (single particle) / Resolution: 4.2 Å EMDB-36140: Cryo-EM structure of Fe-biomineral from bacterioferritin Method: EM (single particle) / Resolution: 5.8 Å
Chemicals	ChemComp-FE2: Unknown entry ChemComp-FE: Unknown entry ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE
Source	streptomyces coelicolor (bacteria)
Keywords	METAL BINDING PROTEIN / Bacterioferritin / OXIDOREDUCTASE