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FEBS Lett. 2004 Jun 4;567(2-3):297-301.

BOF: a novel family of bacterial OB-fold proteins.

Author information

1
Department of Biochemistry, University of Texas, Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA. kginal@chop.swmed.edu

Abstract

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.

PMID:
15178340
DOI:
10.1016/j.febslet.2004.04.086
[Indexed for MEDLINE]
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