Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-Å-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.
|Titolo:||Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170|
RICAGNO, STEFANO (Primo)
|Parole Chiave:||amino acid sequence; bacteriophages; crystallography, x-ray; dna-binding proteins; kinetics; lactococcus lactis; models, molecular; molecular conformation; molecular sequence data; protein conformation; protein structure, tertiary; sequence homology, amino acid; immunology; virology|
|Settore Scientifico Disciplinare:||Settore BIO/10 - Biochimica|
|Data di pubblicazione:||set-2006|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1128/JVI.01160-06|
|Appare nelle tipologie:||01 - Articolo su periodico|