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Let the phage do the work : using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants Teschke CM; Parent KNVirology 2010[Jun]; 401 (2): 119-30The amino acid sequence of viral capsid proteins contains information about their folding, structure and self-assembly processes. While some viruses assemble from small preformed oligomers of coat proteins, other viruses such as phage P22 and herpesvirus assemble from monomeric proteins (Fuller and King, 1980; Newcomb et al., 1999). The subunit assembly process is strictly controlled through protein:protein interactions such that icosahedral structures are formed with specific symmetries, rather than aberrant structures. dsDNA viruses commonly assemble by first forming a precursor capsid that serves as a DNA packaging machine (Earnshaw, Hendrix, and King, 1980; Heymann et al., 2003). DNA packaging is accompanied by a conformational transition of the small precursor procapsid into a larger capsid for isometric viruses. Here we highlight the pseudo-atomic structures of phage P22 coat protein and rationalize several decades of data about P22 coat protein folding, assembly and maturation generated from a combination of genetics and biochemistry.|*Protein Folding[MESH]|*Protein Multimerization[MESH]|Bacteriophage P22/*chemistry/genetics[MESH]|Capsid Proteins/*chemistry/genetics/metabolism[MESH]|Models, Biological[MESH]|Mutant Proteins/*chemistry/genetics/metabolism[MESH]|Virus Assembly[MESH] |
