Structure-function relationships in a bacterial DING protein

FEBS Lett. 2007 Jul 24;581(18):3455-60. doi: 10.1016/j.febslet.2007.06.050. Epub 2007 Jun 27.


A recombinant DING protein from Pseudomonas fluorescens has been previously shown to have a phosphate-binding site, and to be mitogenic for human cells. Here we report the three-dimensional structure of the protein, confirming a close similarity to the "Venus flytrap" structure seen in other human and bacterial phosphate-binding proteins. Site-directed mutagenesis confirms the role of a key residue involved in phosphate binding, and that the mitogenic activity is not dependent on this property. Deletion of one of the two hinged domains that constitute the Venus flytrap also eliminates phosphate binding whilst enhancing mitogenic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Cells, Cultured
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation / genetics
  • Phosphates / chemistry
  • Phosphates / metabolism
  • Protein Folding
  • Protein Structure, Tertiary
  • Pseudomonas fluorescens / chemistry
  • Pseudomonas fluorescens / genetics
  • Pseudomonas fluorescens / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Structural Homology, Protein


  • Bacterial Proteins
  • Phosphates
  • Recombinant Proteins