PROSITE documentation PDOC50905Ferritin-like diiron domain profile
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:
- Ferritin (Ftn), an eukaryotic intracellular protein that stores iron in a soluble, nontoxic, readily available form (see <PDOC00181>).
- Bacterioferritin (Bfr), a prokaryotic protein which may perform functions in iron detoxification and storage.
- Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulfate- reducing bacteria.
- Nigerythrin (Nr), a prokaryotic protein of unknown function.
The profile we developed covers the entire ferritin-like diiron domain.
Last update:April 2003 / First entry.
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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). |
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