BOF: a novel family of bacterial OB-fold proteins

FEBS Lett. 2004 Jun 4;567(2-3):297-301. doi: 10.1016/j.febslet.2004.04.086.


Using top-of-the-line fold recognition methods, we assigned an oligonucleotide/oligosaccharide-binding (OB)-fold structure to a family of previously uncharacterized hypothetical proteins from several bacterial genomes. This novel family of bacterial OB-fold (BOF) proteins present in a number of pathogenic strains encompasses sequences of unknown function from DUF388 (in Pfam database) and COG3111. The BOF proteins can be linked evolutionarily to other members of the OB-fold nucleic acid-binding superfamily (anticodon-binding and single strand DNA-binding domains), although they probably lack nucleic acid-binding properties as implied by the analysis of the potential binding site. The presence of conserved N-terminal predicted signal peptide indicates that BOF family members localize in the periplasm where they may function to bind proteins, small molecules, or other typical OB-fold ligands. As hypothesized for the distantly related OB-fold containing bacterial enterotoxins, the loss of nucleotide-binding function and the rapid evolution of the BOF ligand-binding site may be associated with the presence of BOF proteins in mobile genetic elements and their potential role in bacterial pathogenicity.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Anticodon
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Databases, Protein
  • Genome, Bacterial
  • Models, Molecular
  • Molecular Sequence Data
  • Oligonucleotides / metabolism
  • Oligosaccharides / metabolism
  • Phylogeny
  • Protein Folding
  • Protein Structure, Tertiary
  • Sequence Alignment


  • Anticodon
  • Bacterial Proteins
  • Oligonucleotides
  • Oligosaccharides