Structural highlights
Publication Abstract from PubMed
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-A-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.
Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170.,Ricagno S, Campanacci V, Blangy S, Spinelli S, Tremblay D, Moineau S, Tegoni M, Cambillau C J Virol. 2006 Sep;80(18):9331-5. PMID:16940545[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ricagno S, Campanacci V, Blangy S, Spinelli S, Tremblay D, Moineau S, Tegoni M, Cambillau C. Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170. J Virol. 2006 Sep;80(18):9331-5. PMID:16940545 doi:http://dx.doi.org/80/18/9331
