{PDOC50905}
{PS50905; FERRITIN_LIKE}
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* Ferritin-like diiron domain profile *
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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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2003 / First entry.

[ 1] deMare F., Kurtz D.M. Jr., Nordlund P.
     "The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique
     combination of rubredoxin-like FeS4 and ferritin-like diiron
     domains."
     Nat. Struct. Biol. 3:539-546(1996).
     PubMed=8646540
[ 2] Bonomi F., Kurtz D.M. Jr., Cui X.
     J. Biol. Inorg. Chem. 1:67-72(1996).
[ 3] Kurtz D.M. Jr.
     J. Biol. Inorg. Chem. 2:159-167(1997).

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