8eao
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Cryo-EM structure of the in-situ gp1-gp4 complex from bacteriophage P22
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Structural highlights
FunctionEXLYS_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 | ||||||||||||||||||
This page was last modified 06:20, 6 September 2023.