Crystal Structure of a Chimeric Receptor Binding Protein Constructed from Two Lactococcal Phages

• DOI: 10.1128/jb.01637-08
• Publication Date: 2009-03-14T00:49:30Z
• Authors: Marina Siponen; Silvia Spinelli; Stéphanie Blangy; Sylvain Moineau; Christian Cambillau; Valérie Campanacci
• Keywords: Linker

ABSTRACT Lactococcus lactis , a gram-positive bacterium widely used by the dairy industry to manufacture cheeses, is subject infection diverse population of virulent phages. We have previously determined structures three receptor binding proteins (RBPs) from lactococcal phages TP901-1, p2, and bIL170, each them having distinct host range. Virulent p2 bIL170 are classified within 936 group, while temperate phage TP901-1 member genetically P335 polythetic group. These RBPs comprise domains: N-terminal domain, virion particle; β-helical linker domain; C-terminal bearing site for recognition. Here, we designed, expressed, structure an RBP chimera in which domains (P335) fused domain (936). This exhibits stable that closely resembles parental structures, slight displacement made adaptation efficient. The structurally indistinguishable native binds glycerol with excellent affinity.