Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC50905Ferritin-like diiron domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/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:
- 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.
-------------------------------------------------------------------------------
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). |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.