6E3C

NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein

6E3C の概要

• エントリーDOI: 10.2210/pdb6e3c/pdb
• NMR情報: BMRB: 27435
• 分子名称: Dec protein (1 entity in total)
• 機能のキーワード: cementing, ob-fold, decoration, viral protein
• 由来する生物種: Enterobacteria phage L
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14374.68

構造登録者

Newcomer, R.L.,Alexandrescu, A.T.,Teschke, C.M. (登録日: 2018-07-13, 公開日: 2019-04-17, 最終更新日: 2024-05-15)

主引用文献

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

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: 30945633
DOI: 10.7554/eLife.45345

実験手法

SOLUTION NMR