Revelation of endogenously bound Fe2+ ions in the crystal structure of ferritin from Escherichia coli

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

“…Ferritins are generally pierced by threefold and fourfold channels at their axis points, allowing iron or other small molecules to enter and exit the protein cage [8]. In particular, hydrophilic and hydrophobic pores across ferritin could be responsible for the entry and stable storage of iron [9]. The proteins have approximate interior and exterior diameters of 8 and 12 nm, respectively.…”

The Cation Diffusion Facilitator Family Protein EmfA Confers Resistance to Manganese Toxicity in Brucella abortus 2308 and Is an Essential Virulence Determinant in Mice

“…Metal-responsive transcriptional regulators, for instance, control the expression of metal acquisition systems to ensure these systems operate only under conditions of metal deprivation and ensure that metal exporters are only functional under conditions of metal excess. Furthermore, bacterial species encode metal-specific chaperones to facilitate proper protein metalation (10) and storage proteins to protect against uncontrolled reactivity of intracellular metals (11).…”