BOF: A novel family of bacterial OB-fold proteins

Krzysztof Ginalski, Lisa Kinch, Leszek Rychlewski, Nick V. Grishin

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)297-301
Number of pages5
JournalFEBS Letters
Issue number2-3
StatePublished - Jun 4 2004


  • Bacterial pathogenicity
  • Binding site
  • Fold recognition
  • OB-fold
  • Structure-functional assignment

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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