1DPS

THE CRYSTAL STRUCTURE OF DPS, A FERRITIN HOMOLOG THAT BINDS AND PROTECTS DNA

Summary for 1DPS

• Entry DOI: 10.2210/pdb1dps/pdb
• Descriptor: DPS, SODIUM ION (3 entities in total)
• Functional Keywords: dna-binding protein, ferritin, iron sequestration, stationary phase, oxidative damage, dna binding protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm, nucleoid: P0ABT2
• Total number of polymer chains: 12
• Total formula weight: 225112.19

Authors

Grant, R.A.,Filman, D.J.,Finkel, S.E.,Kolter, R.,Hogle, J.M. (deposition date: 1998-02-23, release date: 1998-09-16, Last modification date: 2024-02-07)

Primary citation

Grant, R.A.,Filman, D.J.,Finkel, S.E.,Kolter, R.,Hogle, J.M.
The crystal structure of Dps, a ferritin homolog that binds and protects DNA.
Nat.Struct.Biol., 5:294-303, 1998

PubMed Abstract: The crystal structure of Dps, a DNA-binding protein from starved E. coli that protects DNA from oxidative damage, has been solved at 1.6 A resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group symmetry which also has a hollow core and pores at the three-folds. The structure suggests a novel DNA-binding motif and a mechanism for DNA protection based on the sequestration of Fe ions.

PubMed: 9546221
DOI: 10.1038/nsb0498-294

Experimental method

X-RAY DIFFRACTION (1.6 Å)