7VI9

Cryo-EM structure of bacteriophage lambda procapsid at 5.03 Angstrom

7VI9 の概要

• エントリーDOI: 10.2210/pdb7vi9/pdb
• EMDBエントリー: 32004
• 分子名称: Major capsid protein (1 entity in total)
• 機能のキーワード: bacteriophage lambda; capsid; procapsid; capsid maturation; virus structure; cryo-em; auxiliary protein; conformational expansion; cementing protein; dna packaging, virus
• 由来する生物種: Escherichia phage lambda (Bacteriophage lambda)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 267604.12

構造登録者

Wang, J.W. (登録日: 2021-09-26, 公開日: 2021-12-15, 最終更新日: 2024-06-19)

主引用文献

Wang, C.,Zeng, J.,Wang, J.
Structural basis of bacteriophage lambda capsid maturation.
Structure, 30:637-, 2022

PubMed Abstract: Bacteriophage lambda is an excellent model system for studying capsid assembly of double-stranded DNA (dsDNA) bacteriophages, some dsDNA archaeal viruses, and herpesviruses. HK97 fold coat proteins initially assemble into a precursor capsid (procapsid) and subsequent genome packaging triggers morphological expansion of the shell. An auxiliary protein is required to stabilize the expanded capsid structure. To investigate the capsid maturation mechanism, we determined the cryo-electron microscopy structures of the bacteriophage lambda procapsid and mature capsid at 3.88 Å and 3.76 Å resolution, respectively. Besides primarily rigid body movements of common features of the major capsid protein gpE, large-scale structural rearrangements of other domains occur simultaneously. Assembly of intercapsomers within the procapsid is facilitated by layer-stacking effects at 3-fold vertices. Upon conformational expansion of the capsid shell, the missing top layer is fulfilled by cementing the gpD protein against the internal pressure of DNA packaging. Our structures illuminate the assembly mechanisms of dsDNA viruses.

PubMed: 35026161
DOI: 10.1016/j.str.2021.12.009

実験手法

ELECTRON MICROSCOPY (5.03 Å)