3LJ5

Full Length Bacteriophage P22 Portal Protein

3LJ5 の概要

• エントリーDOI: 10.2210/pdb3lj5/pdb
• 関連するPDBエントリー: 3LJ4
• 分子名称: Portal protein (1 entity in total)
• 機能のキーワード: portal protein, dna ejection, molecular motor, dna packaging, podoviridae, virus assembly, tail tube, trunk domain, late protein, viral protein
• 由来する生物種: Enterobacteria phage P22 (Bacteriophage P22)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 993952.50

構造登録者

Olia, A.S.,Cingolani, G. (登録日: 2010-01-25, 公開日: 2011-04-20, 最終更新日: 2024-02-21)

主引用文献

Olia, A.S.,Prevelige, P.E.,Johnson, J.E.,Cingolani, G.
Three-dimensional structure of a viral genome-delivery portal vertex.
Nat.Struct.Mol.Biol., 18:597-603, 2011

PubMed Abstract: DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Here, we report two snapshots of the dodecameric portal protein of bacteriophage P22. The 3.25-Å-resolution structure of the portal-protein core bound to 12 copies of gene product 4 (gp4) reveals a ~1.1-MDa assembly formed by 24 proteins. Unexpectedly, a lower-resolution structure of the full-length portal protein unveils the unique topology of the C-terminal domain, which forms a ~200-Å-long α-helical barrel. This domain inserts deeply into the virion and is highly conserved in the Podoviridae family. We propose that the barrel domain facilitates genome spooling onto the interior surface of the capsid during genome packaging and, in analogy to a rifle barrel, increases the accuracy of genome ejection into the host cell.

PubMed: 21499245
DOI: 10.1038/nsmb.2023

実験手法

X-RAY DIFFRACTION (7.497 Å)