Elucidating double stranded DNA viral scaffolding protein structures through advances in cryogenic electron...

Icosahedral double stranded DNA (dsDNA) virus assembly first necessitates the formation of a precursor capsid (procapsid) into which the DNA is packaged. Direct interactions between the major capsid protein (MCP) and a scaffolding protein promote proper procapsid assembly. The scaffolding protein can be an independent protein or a scaffolding-like domain covalently attached to the MCP that is comparable in structure and function. A full understanding of scaffolding protein structures has been limited by their intrinsically disordered nature. Advances in cryogenic electron microscopy (cryoEM) data processing techniques have provided new methodologies to help solve the structures of scaffolding proteins within procapsids. These structural insights further our understanding of how scaffolding proteins interact with the other assembly proteins to correctly construct the procapsid.