Rubrerythrin domain is a nonheme iron binding domain found in many air-sensitive bacteria and archaea and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The homodimeric rubrerythrin protein contains a binuclear metal center located within a four helix bundle. Many, but not all, rubrerythrin proteins have a second domain with a rubredoxin-like hexacoordinated iron center. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system but its function is still poorly understood.
Structure:1B71_A; Desulfovibrio vulgaris Rubrerythrin binds one iron and one zinc atom - View structure with Cn3D
Comment:Rubrerythrin appears to be able to change the ligand arrangements of one of its binding sites to bind different metals under different conditions.
Lu S et al.(2020). "CDD/SPARCLE: the conserved domain database in 2020.",