Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1)

• DOI: 10.1074/jbc.m110.157529
• Publication Date: 2010-09-16T00:27:01Z
• Authors: David Veesler; Gautier Robin; Julie Lichière; Isabelle Auzat; Paulo Tavares; Patrick Bron; Valérie Campanacci; Christian Cambillau
• Keywords: Random hexamer; Negative stain

Siphophage SPP1 infects the gram-positive bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low resolution assignment of most orf products belonging to these regions. We report here structure distal protein (Dit, gp19.1). The combination x-ray crystallography, EM, light scattering established that Dit is back-to-back dimer hexamers. However, fitting in virion EM maps was only possible with hexamer located between tail-tube Structure comparison revealed high similarity central component lactophage baseplates. Sequence search expanded relatedness several phage proteins, suggesting docking platform for adsorption apparatus Siphoviridae infecting bacteria architecture paradigm hub proteins. structural extends also contractile proteins (gpV(N) XkdM) as well components bacterial type 6 secretion system, supporting an evolutionary connection all devices.