The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits.

ABSTRACT: Iron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe²⁺ at binuclear iron ferroxidase centers (FOC) and store the Fe³⁺ in their interior, thus protecting cells from unwanted Fe³⁺/Fe²⁺ redox cycling and storing iron at concentrations far above the solubility of Fe³⁺. Vertebrate ferritins are heteropolymers of H and L subunits with only the H subunits having FOC. Bfr and Ftn were thought to coexist in bacteria as homopolymers, but recent evidence indicates these molecules are heteropolymers assembled from Bfr and Ftn subunits. Despite the heteropolymeric nature of vertebrate and bacterial ferritins, stru

SUBMITTER: Yao H 

PROVIDER: S-EPMC11303784 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature