6QWP

Crystal structure of T7 bacteriophage portal protein, 13mer, closed valve

6QWP の概要

• エントリーDOI: 10.2210/pdb6qwp/pdb
• 関連するPDBエントリー: 6QX5 6QXM 6R21
• EMDBエントリー: 4667 4669 4706
• 分子名称: Portal protein (1 entity in total)
• 機能のキーワード: viral protein, dna packaging
• 由来する生物種: Enterobacteria phage T7
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 785959.03

構造登録者

Fabrega-Ferrer, M.,Cuervo, A.,Machon, C.,Fernandez, F.J.,Perez-Luque, R.,Pous, J.,Vega, M.C.,Carrascosa, J.L.,Coll, M. (登録日: 2019-03-06, 公開日: 2019-09-04, 最終更新日: 2024-05-15)

主引用文献

Cuervo, A.,Fabrega-Ferrer, M.,Machon, C.,Conesa, J.J.,Fernandez, F.J.,Perez-Luque, R.,Perez-Ruiz, M.,Pous, J.,Vega, M.C.,Carrascosa, J.L.,Coll, M.
Structures of T7 bacteriophage portal and tail suggest a viral DNA retention and ejection mechanism.
Nat Commun, 10:3746-3746, 2019

PubMed Abstract: Double-stranded DNA bacteriophages package their genome at high pressure inside a procapsid through the portal, an oligomeric ring protein located at a unique capsid vertex. Once the DNA has been packaged, the tail components assemble on the portal to render the mature infective virion. The tail tightly seals the ejection conduit until infection, when its interaction with the host membrane triggers the opening of the channel and the viral genome is delivered to the host cell. Using high-resolution cryo-electron microscopy and X-ray crystallography, here we describe various structures of the T7 bacteriophage portal and fiber-less tail complex, which suggest a possible mechanism for DNA retention and ejection: a portal closed conformation temporarily retains the genome before the tail is assembled, whereas an open portal is found in the tail. Moreover, a fold including a seven-bladed β-propeller domain is described for the nozzle tail protein.

PubMed: 31431626
DOI: 10.1038/s41467-019-11705-9

実験手法

X-RAY DIFFRACTION (3.4 Å)