6E3C
NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein
Summary for 6E3C
| Entry DOI | 10.2210/pdb6e3c/pdb |
| NMR Information | BMRB: 27435 |
| Descriptor | Dec protein (1 entity in total) |
| Functional Keywords | cementing, ob-fold, decoration, viral protein |
| Biological source | Enterobacteria phage L |
| Total number of polymer chains | 1 |
| Total formula weight | 14374.68 |
| Authors | Newcomer, R.L.,Alexandrescu, A.T.,Teschke, C.M. (deposition date: 2018-07-13, release date: 2019-04-17, Last modification date: 2024-05-15) |
| Primary citation | Newcomer, R.L.,Schrad, J.R.,Gilcrease, E.B.,Casjens, S.R.,Feig, M.,Teschke, C.M.,Alexandrescu, A.T.,Parent, K.N. The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy. Elife, 8:-, 2019 Cited by PubMed Abstract: 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. PubMed: 30945633DOI: 10.7554/eLife.45345 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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