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

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

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 for...

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Bibliographic Details
Main Authors: Rebecca L Newcomer, Jason R Schrad, Eddie B Gilcrease, Sherwood R Casjens, Michael Feig, Carolyn M Teschke, Andrei T Alexandrescu, Kristin N Parent
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2019-04-01
Series:eLife
Subjects:
bacteriophage
nanotechnology
cementing protein
capsid stability
homology modeling
beta-helix
Online Access:https://elifesciences.org/articles/45345

Internet

https://elifesciences.org/articles/45345

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