6RTL

BACTERIOPHAGE SPP1 PROCAPSID-II PROTEIN

6RTL の概要

• エントリーDOI: 10.2210/pdb6rtl/pdb
• EMDBエントリー: 10002 4716 4717
• 分子名称: Major capsid protein (1 entity in total)
• 機能のキーワード: bacteriophage, maturation process, cryo electron microscopy, capsid protein, 3d reconstruction, virus
• 由来する生物種: Bacillus phage SPP1
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 246808.98

構造登録者

Ignatiou, A.,Brasiles, S.,El Sadek, M.,Buerger, J.,Mielke, T.,Topf, M.,Tavares, P. (登録日: 2019-05-24, 公開日: 2019-10-23, 最終更新日: 2024-05-22)

主引用文献

Ignatiou, A.,Brasiles, S.,El Sadek Fadel, M.,Burger, J.,Mielke, T.,Topf, M.,Tavares, P.,Orlova, E.V.
Structural transitions during the scaffolding-driven assembly of a viral capsid.
Nat Commun, 10:4840-4840, 2019

PubMed Abstract: Assembly of tailed bacteriophages and herpesviruses starts with formation of procapsids (virion precursors without DNA). Scaffolding proteins (SP) drive assembly by chaperoning the major capsid protein (MCP) to build an icosahedral lattice. Here we report near-atomic resolution cryo-EM structures of the bacteriophage SPP1 procapsid, the intermediate expanded procapsid with partially released SPs, and the mature capsid with DNA. In the intermediate state, SPs are bound only to MCP pentons and to adjacent subunits from hexons. SP departure results in the expanded state associated with unfolding of the MCP N-terminus and straightening of E-loops. The newly formed extensive inter-capsomere bonding appears to compensate for release of SPs that clasp MCP capsomeres together. Subsequent DNA packaging instigates bending of MCP A domain loops outwards, closing the hexons central opening and creating the capsid auxiliary protein binding interface. These findings provide a molecular basis for the sequential structural rearrangements during viral capsid maturation.

PubMed: 31649265
DOI: 10.1038/s41467-019-12790-6

実験手法

ELECTRON MICROSCOPY (4.2 Å)