Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation


Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or 'procapsid') built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrangement of the coat protein and release of scaffolding protein, resulting in dramatic procapsid lattice expansion… (More)
DOI: 10.1038/ncomms14310


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