View source for Bacterioferritin

{{Cleanup|date=July 2006}}

'''Bacterioferritin''' (BFR) is an oligomeric [[protein]] containing both a binuclear iron center and haem b. The [[tertiary structure]] and [[quaternary structure]] of BFR is very similar to that of [[ferritin]].  The full physiological functions of BFR, which may extend past [[iron]] uptake, are not known. BFR consists of 24 identical subunits that incorporate 12 haem groups and form a roughly spherical, hollow shell.  Iron is stored as a hydrated ferric oxide mineral in its central cavity (about 80 Å diameter).  The overall complex has cubic (432) symmetry.  Each subunit includes a binuclear metalbinding site (the diiron site) linking together the four major helices of the subunit, which has been identified as the ferroxidase [[active site]]. 

BFR from ''[[Pseudomonas aeruginosa]]'', unlike other BFRs, is found to contain two subunit types, which differ considerably in their amino acid sequences. A similar hetero-assembly is seen in the ferritins of higher eukaryotes.

{{PDB|1bfr}}{{PDB|1bcf}}

==External links==
* {{MeshName|bacterioferritin}}

{{Iron-binding proteins}}

[[Category:Proteins]]
[[Category:Enzymes]]


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