Structural rearrangements in the phage head-to-tail interface during assembly and infection.

ABSTRACT: Many icosahedral viruses use a specialized portal vertex to control genome encapsidation and release from the viral capsid. In tailed bacteriophages, the portal system is connected to a tail structure that provides the pipeline for genome delivery to the host cell. We report the first, to our knowledge, subnanometer structures of the complete portal-phage tail interface that mimic the states before and after DNA release during phage infection. They uncover structural rearrangements associated with intimate protein-DNA interactions. The portal protein gp6 of bacteriophage SPP1 undergoes a concerted reorganization of the structural elements of its central channel during interaction with DNA. A network of protein-protein interactions primes consecutive binding of proteins gp15 and gp16 to ext

SUBMITTER: Chaban Y 

PROVIDER: S-EPMC4460457 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature