Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1): A BASEPLATE HUB PARADIGM IN GRAM-POSITIVE INFECTING PHAGES

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 protei...

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Bibliographic Details
Published in:The Journal of biological chemistry 2010-11, Vol.285 (47), p.36666-36673
Main Authors: Veesler, David, Robin, Gautier, Lichière, Julie, Auzat, Isabelle, Tavares, Paulo, Bron, Patrick, Campanacci, Valérie, Cambillau, Christian
Format: Article
Language:English
Subjects:
Adsorption
Bacillus subtilis
Bacillus subtilis - virology
Bacteriophages - genetics
Bacteriophages - metabolism
Contractility
Crystal structure
Crystallography, X-Ray
Electron microscopy
Evolution
Gram-positive bacteria
hexamers
Light scattering
Phages
Protein Conformation
Protein Structure and Folding
Secretion
Siphoviridae
Siphoviridae - genetics
Tails
Viral Regulatory and Accessory Proteins
Viral Tail Proteins - chemistry
Viral Tail Proteins - genetics
Viral Tail Proteins - metabolism
Virion - metabolism
Virions
X-ray crystallography
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Summary: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 (gpVN and XkdM) as well as to components of the bacterial type 6 secretion system, supporting an evolutionary connection between all these devices.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.157529