|PROSITE documentation PDOC50905|
The ferritin-like domain is an about 145-residue domain made of a four-helix bundle surrounding a non-heme, non-sulfur, oxo-bridged diiron site (see <PDB:1RYT>). The diiron site is contained within a twisted, left-handed four-helix-bundle constituted of two anti-parallel helix pairs connected through a left-handed crossover connection. Known ligand residues at non-heme, non-sulfur diiron sites in proteins include His, Asp, Glu, and Tyr. Proteins containing a ferritin-like diiron domain possess the ability to catalyze oxidation of Fe(2+) to Fe(3+) by O2, i.e. ferroxidase activity. The ferritin-like diiron domain occurs in stand-alone form in ferritin and bacterioferritin or in association with the rubredoxin-like domain (see <PDOC50903>) in rubrerythrin [1,2,3].
Proteins known to contain a ferritin-like diiron domain are listed below:
The profile we developed covers the entire ferritin-like diiron domain.Last update:
April 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||deMare F., Kurtz D.M. Jr., Nordlund P.|
|Title||The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.|
|Source||Nat. Struct. Biol. 3:539-546(1996).|
|2||Authors||Bonomi F., Kurtz D.M. Jr., Cui X.|
|Source||J. Biol. Inorg. Chem. 1:67-72(1996).|
|3||Authors||Kurtz D.M. Jr.|
|Source||J. Biol. Inorg. Chem. 2:159-167(1997).|