Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins.

ABSTRACT: Encapsulated ferritins belong to the universally distributed ferritin superfamily, whose members function as iron detoxification and storage systems. Encapsulated ferritins have a distinct annular structure and must associate with an encapsulin nanocage to form a competent iron store that is capable of holding significantly more iron than classical ferritins. The catalytic mechanism of iron oxidation in the ferritin family is still an open question because of the differences in organization of the ferroxidase catalytic site and neighboring secondary metal-binding sites. We have previously identified a putative metal-binding site on the inner surface of the Rhodospirillum rubrum encapsulated ferritin at the interface between the two-helix subunits and proximal to the ferroxidase cent

SUBMITTER: Piergentili C 

PROVIDER: S-EPMC7667983 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature