6QGI

Crystal structure of VP5 from Haloarchaeal pleomorphic virus 2

6QGI の概要

• エントリーDOI: 10.2210/pdb6qgi/pdb
• 分子名称: VP5, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: prokaryotic, viral, membrane fusion, viral protein
• 由来する生物種: Halorubrum pleomorphic virus 2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56878.13

構造登録者

El Omari, K.,Walter, T.S.,Harlos, K.,Grimes, J.M.,Stuart, D.I.,Roine, E. (登録日: 2019-01-11, 公開日: 2019-02-27, 最終更新日: 2024-11-20)

主引用文献

El Omari, K.,Li, S.,Kotecha, A.,Walter, T.S.,Bignon, E.A.,Harlos, K.,Somerharju, P.,De Haas, F.,Clare, D.K.,Molin, M.,Hurtado, F.,Li, M.,Grimes, J.M.,Bamford, D.H.,Tischler, N.D.,Huiskonen, J.T.,Stuart, D.I.,Roine, E.
The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins.
Nat Commun, 10:846-846, 2019

PubMed Abstract: Lipid membrane fusion is an essential function in many biological processes. Detailed mechanisms of membrane fusion and the protein structures involved have been mainly studied in eukaryotic systems, whereas very little is known about membrane fusion in prokaryotes. Haloarchaeal pleomorphic viruses (HRPVs) have a membrane envelope decorated with spikes that are presumed to be responsible for host attachment and membrane fusion. Here we determine atomic structures of the ectodomains of the 57-kDa spike protein VP5 from two related HRPVs revealing a previously unreported V-shaped fold. By Volta phase plate cryo-electron tomography we show that VP5 is monomeric on the viral surface, and we establish the orientation of the molecules with respect to the viral membrane. We also show that the viral membrane fuses with the host cytoplasmic membrane in a process mediated by VP5. This sheds light on protein structures involved in prokaryotic membrane fusion.

PubMed: 30783086
DOI: 10.1038/s41467-019-08728-7

実験手法

X-RAY DIFFRACTION (2.46 Å)