The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy
Year: 2019
Type: article
Abstract: ) and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. These viruses have evolved diverse strategies to fortify their capsids, such as non-covalent binding of auxiliary 'decoration' (Dec) proteins. The Dec protein from the P22-like phage L has a highly unusual binding strategy that distinguishes between nearly identical three-fold and quasi-three-fold sites of the icosahedral capsid. Cryo-electron microscopy and three-dimensional image reconstruction were employed to determine the structure of native phage L particles. NMR was used to determine the structure/dynamics of Dec in solution. The NMR structure and the cryo-EM density envelope were combined to build a model of the capsid-bound Dec trimer. Key regions that modulate the binding interface were verified by site-directed mutagenesis.
Source: eLife
DOI: 10.7554/elife.45345
Language: English
Subfield: Ecology
Field: Environmental Science
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $2,500
Awards: Sf6 as a model system for understanding the mechanisms of virus: host recognition, G3079679661, DNA packaging and delivery by dsDNA viruses, Understanding the Protein: Protein Interactions Required for Virus Assembly, G3643184250, Purchase of a FEI Titan Krios for 3-D EM, G5811413881, G6559513122, Purchase of a direct electron camera for the Titan-Krios at FSU, G8807733469, G9000076857, Modeling and dynamics of biomolecules on cellular scales
OpenAlex ID: W2934857567