Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170
Articolo
Data di Pubblicazione:
2006
Citazione:
Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170 / S. Ricagno, V. Campanacci, S. Blangy, S. Spinelli, D. Tremblay, S. Moineau, M. Tegoni, C. Cambillau. - In: JOURNAL OF VIROLOGY. - ISSN 0022-538X. - 80:18(2006 Sep), pp. 9331-9335.
Abstract:
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
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
Elenco autori:
S. Ricagno, V. Campanacci, S. Blangy, S. Spinelli, D. Tremblay, S. Moineau, M. Tegoni, C. Cambillau
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