Matches in SemOpenAlex for { <https://semopenalex.org/work/W2934857567> ?p ?o ?g. }
- W2934857567 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." @default.
- W2934857567 created "2019-04-11" @default.
- W2934857567 creator A5002233421 @default.
- W2934857567 creator A5006134056 @default.
- W2934857567 creator A5061800523 @default.
- W2934857567 creator A5064937729 @default.
- W2934857567 creator A5065812817 @default.
- W2934857567 creator A5070453901 @default.
- W2934857567 creator A5076907990 @default.
- W2934857567 creator A5081637587 @default.
- W2934857567 date "2019-04-04" @default.
- W2934857567 modified "2023-10-16" @default.
- W2934857567 title "The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy" @default.
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