5OXE

Structure of major capsid protein VP1 of Aeropyrum pernix bacilliform virus 1 APBV1

5OXE の概要

• エントリーDOI: 10.2210/pdb5oxe/pdb
• EMDBエントリー: 3857
• 分子名称: Major virion protein (1 entity in total)
• 機能のキーワード: archaeal virus, thermophile, capsid, helical, virus
• 由来する生物種: Aeropyrum pernix bacilliform virus 1 (isolate -/Japan/Tanaka/2005)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8272.86

構造登録者

Huiskonen, J.T.,Ptchelkine, D.,Phillpps, S.E.V. (登録日: 2017-09-06, 公開日: 2017-11-22, 最終更新日: 2024-05-15)

主引用文献

Ptchelkine, D.,Gillum, A.,Mochizuki, T.,Lucas-Staat, S.,Liu, Y.,Krupovic, M.,Phillips, S.E.V.,Prangishvili, D.,Huiskonen, J.T.
Unique architecture of thermophilic archaeal virus APBV1 and its genome packaging.
Nat Commun, 8:1436-1436, 2017

PubMed Abstract: Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 (Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery.

PubMed: 29127347
DOI: 10.1038/s41467-017-01668-0

実験手法

ELECTRON MICROSCOPY (3.7 Å)