7O6E

2.12 A cryo-EM structure of Mycobacterium tuberculosis Ferritin

Summary for 7O6E

• Entry DOI: 10.2210/pdb7o6e/pdb
• EMDB information: 12738
• Descriptor: Ferritin BfrB (2 entities in total)
• Functional Keywords: iron storage; ferroxidase; bacterial ferritin; octahedral symmetry., metal transport
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 24
• Total formula weight: 491134.46

Authors

Gijsbers, A.,Zhang, Y.,Gao, Y.,Peters, P.J.,Ravelli, R.B.G. (deposition date: 2021-04-10, release date: 2021-05-19, Last modification date: 2024-07-10)

Primary citation

Gijsbers, A.,Zhang, Y.,Gao, Y.,Peters, P.J.,Ravelli, R.B.G.
Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.
Acta Crystallogr D Struct Biol, 77:1077-1083, 2021

PubMed Abstract: The 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 Å 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.

PubMed: 34342280
DOI: 10.1107/S2059798321007233

Experimental method

ELECTRON MICROSCOPY (2.1 Å)