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J. Biol. Chem., Vol. 281, Issue 20, 14256-14262, May 19, 2006

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Modular Structure of the Receptor Binding Proteins of Lactococcus lactis Phages

THE RBP STRUCTURE OF THE TEMPERATE PHAGE TP901-1^*

Silvia Spinelli¹, Valérie Campanacci¹, Stéphanie Blangy, Sylvain Moineau^¶||, Mariella Tegoni, and Christian Cambillau²

From the Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I and II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France and the Groupe de Recherche en Écologie Buccale, Faculté de Médecine Dentaire, the ^¶Félix d'Hérelle Reference Center for Bacterial Viruses, and the ^||Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Université Laval, Québec City, Québec G1K 7P4, Canada

Lactococcus lactis is a Gram-positive bacterium widely used by the dairy industry. Several industrial L. lactis strains are sensitive to various distinct bacteriophages. Most of them belong to the Siphoviridae family and comprise several species, among which the 936 and P335 are prominent. Members of these two phage species recognize their hosts through the interaction of their receptor-binding protein (RBP) with external cell wall saccharidices of the host, the "receptors." We report here the 1.65 Å resolution crystal structure of the RBP from phage TP901-1, a member of the P335 species. This RBP of 163 amino acids is a homotrimer comprising three domains: a helical N terminus, an interlaced -prism, and a -barrel, the head domain (residues 64-163), which binds a glycerol molecule. Fluorescence quenching experiments indicated that the RBP exhibits high affinity for glycerol, muramyl-dipeptide, and other saccharides in solution. The structural comparison of this RBP with that of lactococcal phage p2 RBP, a member of the 936 species (Spinelli, S., Desmyter, A., Verrips, C. T., de Haard, J. W., Moineau, S., and Cambillau, C. (2006) Nat. Struct. Mol. Biol. 13, 85-89) suggests a large extent of modularity in RBPs of lactococcal phages.

Received for publication, January 23, 2006 , and in revised form, March 17, 2006.

The atomic coordinates and structure factors (code 2F0C) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Genopole of Marseille-Nice and by the Natural Sciences and Engineering Research Council of Canada. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed. Fax: 33-491-266-720; E-mail: cambillau{at}afmb.univ-mrs.fr.

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