InterPro : IPR002024

Name  Bacterioferritin Short Name  Bacterioferritin
Type  Family Description  Bacterioferritin (BFR; also known as cytochrome b1 or cytochrome b557) [, ]of Escherichia coliis an iron-storage protein consisting of 24 identicalsubunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter [, ]. X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryotes and bacteria []. Common to both ferritins and BFRs is a capacity to store large quantities of iron within their hollow interior, inthe form of a hydrated ferric oxide mineral containing variable amounts ofphosphate anion. However, a major difference between them is that BFR contains up 12 b-type haem groups, while ferritins, as isolated, do not contain haem. The building block for the BFR shell is a protein dimer (subunits A and B) binding the single haem group. Each subunit consists of four nearly parallel alpha-helices. The haem is bound symmetrically to subunits A and Bby Met(A)-52 and Met(B)-52 residues []. Each subunit includes a binuclear metal-binding site linking together the four major helices of the subunit, which has been identified as the ferroxidase centre of BFR []. BFR mutants with Met-52 replacedare haem-free, but appear to be correctly assembled and are capable of accumulating iron [].
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR012347 Ferritin-related Ferritin-rel Domain
IPR009040 Ferritin- like diiron domain Ferritin-like_diiron Domain

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Le Brun NE Identification of the ferroxidase centre of Escherichia coli bacterioferritin. 1995 Biochem J 312 ( Pt 2) 385-92
Andrews SC Genetic and structural characterization of the bacterioferritin of Escherichia coli. 1990 Biochem Soc Trans 18 658-9
Andrews SC Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii. 1991 Biochim Biophys Acta 1078 111-6
Harrison PM The ferritins: molecular properties, iron storage function and cellular regulation. 1996 Biochim Biophys Acta 1275 161-203
Andrews SC Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants. 1995 J Biol Chem 270 23268-74
Frolow F Structure of a unique twofold symmetric haem-binding site. 1994 Nat Struct Biol 1 453-60



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)