Structural highlights
Function[BFRB_MYCTU] Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.[1] Publication Abstract from PubMedThe use of cryo-EM continues to expand worldwide and calls for good-quality standard proteins with simple protocols for their production. Here, a straightforward expression and purification protocol is presented that provides an apoferritin, bacterioferritin B (BfrB), from Mycobacterium tuberculosis with high yield and purity. A 2.12 A resolution cryo-EM structure of BfrB is reported, showing the typical cage-like oligomer constituting of 24 monomers related by 432 symmetry. However, it also contains a unique C-terminal extension (164-181), which loops into the cage region of the shell and provides extra stability to the protein. Part of this region was ambiguous in previous crystal structures but could be built within the cryo-EM map. These findings and this protocol could serve the growing cryo-EM community in characterizing and pushing the limits of their electron microscopes and workflows. Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.,Gijsbers A, Zhang Y, Gao Y, Peters PJ, Ravelli RBG Acta Crystallogr D Struct Biol. 2021 Aug 1;77(Pt 8):1077-1083. doi:, 10.1107/S2059798321007233. Epub 2021 Jul 29. PMID:34342280[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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