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The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.


ABSTRACT: The major coat proteins of dsDNA tailed phages (order Caudovirales) 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.

SUBMITTER: Newcomer RL 

PROVIDER: S-EPMC6449081 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.

Newcomer Rebecca L RL   Schrad Jason R JR   Gilcrease Eddie B EB   Casjens Sherwood R SR   Feig Michael M   Teschke Carolyn M CM   Alexandrescu Andrei T AT   Parent Kristin N KN  

eLife 20190404


The major coat proteins of dsDNA tailed phages (order <i>Caudovirales</i>) 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 bet  ...[more]

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