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The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin
- Source :
- Biochimica et biophysica acta. 1598(1-2)
- Publication Year :
- 2002
-
Abstract
- 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 α-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.
- Subjects :
- Halobacterium salinarum
Models, Molecular
Structural similarity
Protein Conformation
Archaeal Proteins
Molecular Sequence Data
Biophysics
Biochemistry
Analytical Chemistry
chemistry.chemical_compound
Mole
Metalloproteins
Amino Acid Sequence
FERRIC IRON
Molecular Biology
Protein secondary structure
Heme
biology
Sequence Homology, Amino Acid
biology.organism_classification
Sequence identity
Ferritin
chemistry
Ferritins
biology.protein
Sequence Alignment
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1598
- Issue :
- 1-2
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....1c73f6515f8b8209d562084e8985ba2b