6WXE

Cryo-EM reconstruction of VP5*/VP8* assembly from rhesus rotavirus particles - Upright conformation

これはPDB形式変換不可エントリーです。

6WXE の概要

• エントリーDOI: 10.2210/pdb6wxe/pdb
• EMDBエントリー: 21955
• 分子名称: Outer capsid protein VP4, Intermediate capsid protein VP6, Outer capsid glycoprotein VP7, ... (5 entities in total)
• 機能のキーワード: complex, non-enveloped virus, viral particle, entry, membrane-penetration, rotavirus, vp4, vp5*, vp8*, viral protein
• 由来する生物種: Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A); 詳細
• タンパク質・核酸の鎖数: 39
• 化学式量合計: 1743396.06

構造登録者

Herrmann, T.,Harrison, S.C.,Jenni, S. (登録日: 2020-05-10, 公開日: 2021-01-20, 最終更新日: 2024-11-06)

主引用文献

Herrmann, T.,Torres, R.,Salgado, E.N.,Berciu, C.,Stoddard, D.,Nicastro, D.,Jenni, S.,Harrison, S.C.
Functional refolding of the penetration protein on a non-enveloped virus.
Nature, 590:666-670, 2021

PubMed Abstract: A non-enveloped virus requires a membrane lesion to deliver its genome into a target cell. For rotaviruses, membrane perforation is a principal function of the viral outer-layer protein, VP4. Here we describe the use of electron cryomicroscopy to determine how VP4 performs this function and show that when activated by cleavage to VP8* and VP5*, VP4 can rearrange on the virion surface from an 'upright' to a 'reversed' conformation. The reversed structure projects a previously buried 'foot' domain outwards into the membrane of the host cell to which the virion has attached. Electron cryotomograms of virus particles entering cells are consistent with this picture. Using a disulfide mutant of VP4, we have also stabilized a probable intermediate in the transition between the two conformations. Our results define molecular mechanisms for the first steps of the penetration of rotaviruses into the membranes of target cells and suggest similarities with mechanisms postulated for other viruses.

PubMed: 33442061
DOI: 10.1038/s41586-020-03124-4

実験手法

ELECTRON MICROSCOPY (3.4 Å)