The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin.
An iron-rich protein, DpsA(Hsal), was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 100 Fe ions per mole of holoprotein. CD spectra and secondary structure calculations are consistent with an alpha-helical contribution of 60%. The UV/VIS spectrum provides no evidence for the presence of heme groups. This protein exhibits features of a non-heme type bacterial ferritin (Ftn) although it shares only little sequence homology with Ftn. Molecular modelling disclosed a high structural similarity to E. coli Dps.
Reindel
Sabine
S
Isotopenlabor TNF, Medizinische Universität zu Lübeck, Ratzeburger Allee 160, Lübeck, Germany.
Anemüller
Stefan
S
Sawaryn
Andrzej
A
Matzanke
Berthold F
BF
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D005293:Ferritins / Q000737:chemistry*; D019617:Halobacterium salinarum / Q000737:chemistry*; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D008667:Metalloproteins; D005293:Ferritins