PMID:24097944

Citation	Maxwell, KL, Fatehi Hassanabad, M, Chang, T, Paul, VD, Pirani, N, Bona, D, Edwards, AM and Davidson, AR (2013) Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages. J. Bacteriol. 195:5461-8
Abstract	A variety of bacterial pathogenicity determinants, including the type VI secretion system and the virulence cassettes from Photorhabdus and Serratia, share an evolutionary origin with contractile-tailed myophages. The well-characterized Escherichia coli phage P2 provides an excellent system for studies related to these systems, as its protein composition appears to represent the "minimal" myophage tail. In this study, we used nuclear magnetic resonance (NMR) spectroscopy to determine the solution structure of gpX, a 68-residue tail baseplate protein. Although the sequence and structure of gpX are similar to those of LysM domains, which are a large family associated with peptidoglycan binding, we did not detect a peptidoglycan-binding activity for gpX. However, bioinformatic analysis revealed that half of all myophages, including all that possess phage T4-like baseplates, encode a tail protein with a LysM-like domain, emphasizing a widespread role for this domain in baseplate function. While phage P2 gpX comprises only a single LysM domain, many myophages display LysM domain fusions with other tail proteins, such as the DNA circulation protein found in Mu-like phages and gp53 of T4-like phages. Electron microscopy of P2 phage particles with an incorporated gpX-maltose binding protein fusion revealed that gpX is located at the top of the baseplate, near the junction of the baseplate and tail tube. gpW, the orthologue of phage T4 gp25, was also found to localize to this region. A general colocalization of LysM-like domains and gpW homologues in diverse phages is supported by our bioinformatic analysis.
Links	PubMed PMC3889624 Online version:10.1128/JB.00805-13
Keywords	Bacteriophage P2/chemistry; Bacteriophage P2/physiology; Bacteriophage P2/ultrastructure; Escherichia coli/virology; Glycoproteins/chemistry; Glycoproteins/metabolism; Magnetic Resonance Spectroscopy; Microscopy, Electron; Protein Conformation; Viral Tail Proteins/chemistry; Viral Tail Proteins/metabolism; Virion/chemistry; Virion/ultrastructure
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BPP2:BPX		GO:0098025: virus tail, baseplate	ECO:0000314:		C		Figure 1 shows localization of MBP-tagged gpX to the baseplate of the phage. The higher density observed compared to WT is a consequence of the 367 residue MBP tag on plasmid expressed gpX.	complete CACAO 12019
BPP2:BPW		GO:0098025: virus tail, baseplate	ECO:0000314:		C		Increased area of density in wt, illustrate where gpW is localized in the baseplate as seen in Fig 1.	complete CACAO 12026

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