| Description | This group belongs to the ferritin domain superfamily and has the ferritin-like structural fold. Ferritins constitute a broad superfamily of iron storage proteins, widespread in all domains of life [ , ]. Ferritins and bacterioferritins have essentially the same architecture, assembling in a 24mer cluster to form a hollow, roughly spherical, construction. This consists of a mineral core of hydrated ferric oxide and a multi-subunit protein shell, which encloses the former and assures its solubility in an aqueous environment. Due to the absence of the C-terminal fifth helix of 24mer ferritins, members of the Dps group assemble only to dodecameric protein shells [].Members of this entry were originally discovered as stress proteins, which protect DNA against oxidative stress during nutrient starvation [ ], hence the name Dps (DNA protection during starvation protein). Several members of the group, such as Dps from Escherichia coli or the Dps homologue from Bacillus subtilis, exhibit a DNA-binding activity that is at least partially linked with iron complexation []. DNA binding by these proteins was shown to suffice for protection against oxidative DNA damage and might be mediated by magnesium ions, which bridge the protein surfaces with the polyanionic DNA [, ]. Functionally, this group is much more diverse, with many members promoting iron incorporation, while others act as immunogens, neutrophil activators [], cold-shock proteins, or constituents of fine-tangled pili []. Another mode of protection against reactive oxygen species implies the preferential consumption of hydrogen peroxide instead of oxygen during biomineralization [].For additional information please see [ , ]. | Name | DNA-binding protein Dps |
| Short Name | DPS_DNA-bd | Type | Family |
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