4RGA
Phage 1358 receptor binding protein in complex with the trisaccharide GlcNAc-Galf-GlcOMe
Summary for 4RGA
Entry DOI | 10.2210/pdb4rga/pdb |
Related | 4L92 4L97 4L99 |
Descriptor | Phage 1358 receptor binding protein (ORF20), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-beta-D-galactofuranose-(1-6)-methyl alpha-D-glucopyranoside (3 entities in total) |
Functional Keywords | alpha/beta protein, phage receptor binding protein, lactococcus lactis smq388, viral protein |
Biological source | Lactococcus phage 1358 |
Total number of polymer chains | 2 |
Total formula weight | 87803.09 |
Authors | Spinelli, S.,Mccabe, O.,Farenc, C.,Tremblay, D.,Blangy, S.,Oscarson, S.,Moineau, S.,Cambillau, C. (deposition date: 2014-09-29, release date: 2015-05-20, Last modification date: 2023-09-20) |
Primary citation | McCabe, O.,Spinelli, S.,Farenc, C.,Labbe, M.,Tremblay, D.,Blangy, S.,Oscarson, S.,Moineau, S.,Cambillau, C. The targeted recognition of Lactococcus lactis phages to their polysaccharide receptors. Mol.Microbiol., 96:875-886, 2015 Cited by PubMed Abstract: Each phage infects a limited number of bacterial strains through highly specific interactions of the receptor-binding protein (RBP) at the tip of phage tail and the receptor at the bacterial surface. Lactococcus lactis is covered with a thin polysaccharide pellicle (hexasaccharide repeating units), which is used by a subgroup of phages as a receptor. Using L. lactis and phage 1358 as a model, we investigated the interaction between the phage RBP and the pellicle hexasaccharide of the host strain. A core trisaccharide (TriS), derived from the pellicle hexasaccharide repeating unit, was chemically synthesised, and the crystal structure of the RBP/TriS complex was determined. This provided unprecedented structural details of RBP/receptor site-specific binding. The complete hexasaccharide repeating unit was modelled and found to aptly fit the extended binding site. The specificity observed in in vivo phage adhesion assays could be interpreted in view of the reported structure. Therefore, by combining synthetic carbohydrate chemistry, X-ray crystallography and phage plaquing assays, we suggest that phage adsorption results from distinct recognition of the RBP towards the core TriS or the remaining residues of the hexasacchride receptor. This study provides a novel insight into the adsorption process of phages targeting saccharides as their receptors. PubMed: 25708888DOI: 10.1111/mmi.12978 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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