Autor: |
Rebecca L Newcomer, Jason R Schrad, Eddie B Gilcrease, Sherwood R Casjens, Michael Feig, Carolyn M Teschke, Andrei T Alexandrescu, Kristin N Parent |
Jazyk: |
angličtina |
Rok vydání: |
2019 |
Předmět: |
|
Zdroj: |
eLife, Vol 8 (2019) |
Druh dokumentu: |
article |
ISSN: |
2050-084X |
DOI: |
10.7554/eLife.45345 |
Popis: |
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. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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