Source:http://linkedlifedata.com/resource/pubmed/id/15178340
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
2004-6-4
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pubmed:abstractText |
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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
567
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
297-301
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15178340-Amino Acid Sequence,
pubmed-meshheading:15178340-Anticodon,
pubmed-meshheading:15178340-Bacterial Proteins,
pubmed-meshheading:15178340-Binding Sites,
pubmed-meshheading:15178340-Databases, Protein,
pubmed-meshheading:15178340-Genome, Bacterial,
pubmed-meshheading:15178340-Models, Molecular,
pubmed-meshheading:15178340-Molecular Sequence Data,
pubmed-meshheading:15178340-Oligonucleotides,
pubmed-meshheading:15178340-Oligosaccharides,
pubmed-meshheading:15178340-Phylogeny,
pubmed-meshheading:15178340-Protein Folding,
pubmed-meshheading:15178340-Protein Structure, Tertiary,
pubmed-meshheading:15178340-Sequence Alignment
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pubmed:year |
2004
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pubmed:articleTitle |
BOF: a novel family of bacterial OB-fold proteins.
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pubmed:affiliation |
Department of Biochemistry, University of Texas, Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA. kginal@chop.swmed.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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