Cellular and Molecular Life Sciences

, Volume 67, Issue 3, pp 341–351 | Cite as

Dps-like proteins: structural and functional insights into a versatile protein family



Dps-like proteins are key factors involved in the protection of prokaryotic cells from oxidative damage. They act by either oxidizing iron to prevent the formation of oxidative radicals or by forming Dps-DNA complexes to physically protect DNA. All Dps-like proteins are characterized by a common three-dimensional architecture and are found as spherical dodecamers with a hollow central cavity. Despite their structural similarities, recent biochemical and structural data have suggested different functions among members of the family that range from protection inside the cells in response to various stress signals to adhesion and virulence during bacterial infections. Moreover, the Dps-like proteins have lately attracted considerable interest in the field of nanotechnology owing to their ability to act as protein cages for iron and various other metals. A better understanding of their function and mechanism could therefore lead to novel applications in biotechnology and nanotechnology.


Oxidative stress Mini-ferritins Metal binding Ferroxidase Fenton reaction Iron binding Zinc 

Supplementary material

18_2009_168_MOESM1_ESM.doc (38 kb)
Supplementary, Table SI (DOC 10 kb)
18_2009_168_MOESM2_ESM.tif (14.8 mb)
Figure S1. Sequence alignment of Dps-family representatives. The secondary structures are presented according to E. coli Dps. The blue triangles indicate the iron-binding residues at the mono-iron ferroxidase center. The blue boxes show residues that share at least 70% similarity in physico-chemical properties. Figure was created with ESPript (http://www.espript.ibcp.fr/). (TIF 3391 kb)


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Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009

Authors and Affiliations

  • Teemu Haikarainen
    • 1
  • Anastassios C. Papageorgiou
    • 1
  1. 1.Turku Centre for BiotechnologyUniversity of Turku and Åbo Akademi UniversityTurkuFinland

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