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6D5F

Cryo-EM reconstruction of membrane-enveloped filamentous virus SFV1 (Sulfolobus filamentous virus 1)

6D5F の概要
エントリーDOI10.2210/pdb6d5f/pdb
EMDBエントリー7797
分子名称Fimbrial protein, DNA (336-MER) (3 entities in total)
機能のキーワードfilamentous virus, helical symmetry, membrane enveloped virus, virus
由来する生物種Sulfolobus filamentous virus 1
詳細
タンパク質・核酸の鎖数54
化学式量合計1190477.03
構造登録者
Wang, F.,Osinski, T.,Liu, Y.,Krupovic, M.,Prangishvili, D.,Egelman, E.H. (登録日: 2018-04-19, 公開日: 2018-08-29, 最終更新日: 2024-11-20)
主引用文献Liu, Y.,Osinski, T.,Wang, F.,Krupovic, M.,Schouten, S.,Kasson, P.,Prangishvili, D.,Egelman, E.H.
Structural conservation in a membrane-enveloped filamentous virus infecting a hyperthermophilic acidophile.
Nat Commun, 9:3360-3360, 2018
Cited by
PubMed Abstract: Different forms of viruses that infect archaea inhabiting extreme environments continue to be discovered at a surprising rate, suggesting that the current sampling of these viruses is sparse. We describe here Sulfolobus filamentous virus 1 (SFV1), a membrane-enveloped virus infecting Sulfolobus shibatae. The virus encodes two major coat proteins which display no apparent sequence similarity with each other or with any other proteins in databases. We have used cryo-electron microscopy at 3.7 Å resolution to show that these two proteins form a nearly symmetrical heterodimer, which wraps around A-form DNA, similar to what has been shown for SIRV2 and AFV1, two other archaeal filamentous viruses. The thin (∼ 20 Å) membrane of SFV1 is mainly archaeol, a lipid species that accounts for only 1% of the host lipids. Our results show how relatively conserved structural features can be maintained across evolution by both proteins and lipids that have diverged considerably.
PubMed: 30135568
DOI: 10.1038/s41467-018-05684-6
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.7 Å)
構造検証レポート
Validation report summary of 6d5f
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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