2bsd | pdb_00002bsd
STRUCTURE OF LACTOCOCCAL BACTERIOPHAGE P2 RECEPTOR BINDING PROTEIN
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Overview
Lactococcus 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.
About this Structure
2BSD is a Single protein structure of sequence from Lactococcus lactis phage p475. Full crystallographic information is available from OCA.
Reference
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
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