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The Crystal Structure of Pyocin L1 bound to D-rhamnose at 2.37 AngstromsThe Crystal Structure of Pyocin L1 bound to D-rhamnose at 2.37 Angstroms
Structural highlights
FunctionPublication Abstract from PubMedLectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-specific killing activity. Here we show that pyocin L1, a novel member of this family from Pseudomonas aeruginosa, targets susceptible strains of this species through recognition of the common polysaccharide antigen (CPA) of P. aeruginosa lipopolysaccharide that is predominantly a homopolymer of d-rhamnose. Structural and biophysical analyses show that recognition of CPA occurs through the C-terminal carbohydrate-binding domain of pyocin L1 and that this interaction is a prerequisite for bactericidal activity. Further to this, we show that the previously described lectin-like bacteriocin putidacin L1 shows a similar carbohydrate-binding specificity, indicating that oligosaccharides containing d-rhamnose and not d-mannose, as was previously thought, are the physiologically relevant ligands for this group of bacteriocins. The widespread inclusion of d-rhamnose in the lipopolysaccharide of members of the genus Pseudomonas explains the unusual genus-specific activity of the lectin-like bacteriocins. Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor.,McCaughey LC, Grinter R, Josts I, Roszak AW, Waloen KI, Cogdell RJ, Milner J, Evans T, Kelly S, Tucker NP, Byron O, Smith B, Walker D PLoS Pathog. 2014 Feb 6;10(2):e1003898. doi: 10.1371/journal.ppat.1003898., eCollection 2014 Feb. PMID:24516380[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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