8RT1

BTV15 VP5 at pH 9.0

8RT1 の概要

• エントリーDOI: 10.2210/pdb8rt1/pdb
• 分子名称: Outer capsid protein VP5 (1 entity in total)
• 機能のキーワード: bluetongue virus, outer capsid protein, viral protein
• 由来する生物種: Bluetongue virus 15
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 503324.41

構造登録者

Sutton, G.C.,Stuart, D.I. (登録日: 2024-01-25, 公開日: 2024-09-04, 最終更新日: 2024-10-23)

主引用文献

Zhang, H.,El Omari, K.,Sutton, G.,Stuart, D.I.
The effect of pH on the structure of Bluetongue virus VP5.
J.Gen.Virol., 105:-, 2024

PubMed Abstract: The unenveloped Bluetongue virus capsid comprises several structural layers, the inner two comprising a core, which assembles before addition of the outer proteins, VP2 and VP5. Two symmetric trimers of VP5 fit like pegs into two distinct pits on the core and undergo pH conformational changes in the context of the virus, associated with cell entry. Here we show that in isolation VP5 alone undergoes essentially the same changes with pH and confirm a helical transition, indicating that VP5 is a motor during cell entry. In the absence of VP5 the two pits on the core differ from each other, presumably due to the asymmetric underlying structure of VP3, the innermost capsid protein. On insertion of VP5 these pits become closely similar and remain similar at low pH whilst VP5 is present. This natural asymmetry presumably destabilises the attachment of VP5, facilitating ejection upon low pH, membrane penetration and cell entry.

PubMed: 39163113
DOI: 10.1099/jgv.0.002018

実験手法

X-RAY DIFFRACTION (2.8 Å)