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PROSITE documentation PDOC50905 [for PROSITE entry PS50905] |
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). | |
PubMed ID | 8646540 |
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). |