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American Society for Microbiology, Journal of Virology, 18(80), p. 9331-9335, 2006

DOI: 10.1128/jvi.01160-06

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Crystal Structure of the Receptor-Binding Protein Head Domain from Lactococcus lactis Phage bIL170

Journal article published in 2006 by Stefano Ricagno, Valérie Campanacci ORCID, Stéphanie Blangy, Silvia Spinelli, Denise Tremblay, Sylvain Moineau, Mariella Tegoni, Christian Cambillau
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.