The Crystal Structure of Dps, a Ferritin Homolog That Binds and Protects DNA

Nat Struct Biol. 1998 Apr;5(4):294-303. doi: 10.1038/nsb0498-294.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / physiology
  • Ferritins / chemistry*
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Oxidative Stress
  • Point Mutation
  • Protein Conformation*
  • Protein Folding
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • DPS protein, Bacteria
  • Macromolecular Substances
  • Recombinant Proteins
  • DNA
  • Ferritins

Associated data

  • PDB/1DPS