Structural highlights
Function
EXLYS_BPP22 Tail protein located at the vertex occupied by the portal ring. Together with gp10 and gp26, gp4 is required for stabilization of the condensed DNA within the capsid; perhaps by plugging the hole through which the DNA enters. Plays a role in ejection of the bacteriophage DNA into the host cell at the initiation of infection. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans.[1]
References
- ↑ Moak M, Molineux IJ. Peptidoglycan hydrolytic activities associated with bacteriophage virions. Mol Microbiol. 2004 Feb;51(4):1169-83. PMID:14763988
