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TitleThe phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateApr 4, 2019
AuthorsRebecca L Newcomer / Jason R Schrad / Eddie B Gilcrease / Sherwood R Casjens / Michael Feig / Carolyn M Teschke / Andrei T Alexandrescu / Kristin N Parent /
PubMed AbstractThe major coat proteins of dsDNA tailed phages (order ) and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by ...The major coat proteins of dsDNA tailed phages (order ) 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.
External linksElife / PubMed:30945633 / PubMed Central
MethodsEM (single particle) / NMR (solution)
Resolution4.2 Å
Structure data

EMDB-9392:
Bacteriophage L virion
Method: EM (single particle) / Resolution: 4.2 Å

PDB-6e3c:
NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein
Method: SOLUTION NMR

Source
  • enterobacteria phage l (virus)
KeywordsVIRAL PROTEIN / Cementing / OB-Fold / Decoration

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