4LED

The Crystal Structure of Pyocin L1 bound to D-rhamnose at 2.37 Angstroms

Summary for 4LED

• Entry DOI: 10.2210/pdb4led/pdb
• Related: 4LE7 4LEA 4LED
• Descriptor: Pyocin L1, alpha-D-rhamnopyranose (3 entities in total)
• Functional Keywords: monocot mannose binding protein, galanthus nivalis agglutinin, beta prism, bacteriocin, antimicrobial protein, extracellular, sugar binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 61165.13

Authors

Grinter, R.,Roszak, A.W.,Mccaughey, L.,Cogdell, C.J.,Walker, D. (deposition date: 2013-06-25, release date: 2014-02-19, Last modification date: 2023-09-20)

Primary citation

McCaughey, L.C.,Grinter, R.,Josts, I.,Roszak, A.W.,Walen, K.I.,Cogdell, R.J.,Milner, J.,Evans, T.,Kelly, S.,Tucker, N.P.,Byron, O.,Smith, B.,Walker, D.
Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor.
Plos Pathog., 10:e1003898-e1003898, 2014

PubMed Abstract: Lectin-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.

PubMed: 24516380
DOI: 10.1371/journal.ppat.1003898

Experimental method

X-RAY DIFFRACTION (2.37 Å)