2bsd
Structure of Lactococcal Bacteriophage p2 Receptor Binding Protein
Structural highlights
FunctionRBP_BPLP2 Binds to the host phosphopolysaccharides at the onset of infection. Upon activation by calcium, the receptor binding proteins change their conformation, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA ejection.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLactococcus lactis is a Gram-positive bacterium used extensively by the dairy industry for the manufacture of fermented milk products. The double-stranded DNA bacteriophage p2 infects specific L. lactis strains using a receptor-binding protein (RBP) located at the tip of its noncontractile tail. We have solved the crystal structure of phage p2 RBP, a homotrimeric protein composed of three domains: the shoulders, a beta-sandwich attached to the phage; the neck, an interlaced beta-prism; and the receptor-recognition head, a seven-stranded beta-barrel. We used the complex of RBP with a neutralizing llama VHH domain to identify the receptor-binding site. Structural similarity between the recognition-head domain of phage p2 and those of adenoviruses and reoviruses, which invade mammalian cells, suggests that these viruses, despite evolutionary distant targets, lack of sequence similarity and the different chemical nature of their genomes (DNA versus RNA), might have a common ancestral gene. Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses.,Spinelli S, Desmyter A, Verrips CT, de Haard HJ, Moineau S, Cambillau C Nat Struct Mol Biol. 2006 Jan;13(1):85-9. Epub 2005 Dec 4. PMID:16327804[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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