Structural highlights
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 PubMedSiphophage SPP1 infects the Gram+ 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 the structure of the SPP1 distal tail protein (Dit, gp19.1). The combination of X-ray crystallography, EM and light scattering established that Dit is a back-to-back dimer of hexamers. However, Dit fitting in the virion EM maps was only possible with a hexamer located between the tail-tube and the tail-tip. Structure comparison revealed high similarity between Dit and a central component of lactophage baseplates. Sequence similarity search expanded its relatedness to several phage proteins, suggesting that Dit is a docking platform for the tail adsorption apparatus in Siphoviridae infecting Gram+ bacteria and that its architecture is a paradigm for these hub proteins. Dit structural similarity extends also to non-contractile and contractile phage tail proteins (gpVN and XkdM) as well as to components of the bacterial type 6 secretion system, supporting an evolutionary connection between all these devices. Crystal structure of bacteriophage SPP1 distal tail protein (GP 19.1): a baseplate hub paradigm in gram+ infecting phages.,Veesler D, Robin G, Lichiere J, Auzat I, Tavares P, Bron P, Campanacci V, Cambillau C J Biol Chem. 2010 Sep 15. PMID:20843802[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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