2X8K

Crystal Structure of SPP1 Dit (gp 19.1) Protein, a Paradigm of Hub Adsorption Apparatus in Gram-positive Infecting Phages.

Summary for 2X8K

• Entry DOI: 10.2210/pdb2x8k/pdb
• Descriptor: HYPOTHETICAL PROTEIN 19.1 (1 entity in total)
• Functional Keywords: viral protein, distal tail protein
• Biological source: BACILLUS PHAGE SPP1
• Total number of polymer chains: 3
• Total formula weight: 85287.04

Authors

Veesler, D.,Robin, G.,Lichiere, J.,Auzat, I.,Tavares, P.,Bron, P.,Campanacci, V.,Cambillau, C. (deposition date: 2010-03-10, release date: 2010-09-15, Last modification date: 2024-05-08)

Primary citation

Veesler, D.,Robin, G.,Lichiere, J.,Auzat, I.,Tavares, P.,Bron, P.,Campanacci, V.,Cambillau, C.
Crystal Structure of Bacteriophage Spp1 Distal Tail Protein (Gp 19.1): A Baseplate Hub Paradigm in Gram+ Infecting Phages.
J.Biol.Chem., 285:36666-, 2010

PubMed Abstract: 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 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-positive 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 (gpV(N) and XkdM) as well as to components of the bacterial type 6 secretion system, supporting an evolutionary connection between all these devices.

PubMed: 20843802
DOI: 10.1074/JBC.M110.157529

Experimental method

X-RAY DIFFRACTION (2.95 Å)