6OUT

Asymmetric focused reconstruction of human norovirus GI.1 Norwalk strain VLP asymmetric unit in T=3 symmetry

6OUT の概要

• エントリーDOI: 10.2210/pdb6out/pdb
• 関連するPDBエントリー: 6OTF
• EMDBエントリー: 20195 20197 20198 20199 20201 20202 20205 20206
• 分子名称: Capsid protein VP1 (2 entities in total)
• 機能のキーワード: caliciviridae, norovirus, gi.1, norwalk, virus like particle
• 由来する生物種: Norwalk virus (strain GI/Human/United States/Norwalk/1968) (Hu/NV/NV/1968/US)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 169889.48

構造登録者

Jung, J.,Grant, T.,Thomas, D.R.,Diehnelt, C.W.,Grigorieff, N.,Joshua-Tor, L. (登録日: 2019-05-05, 公開日: 2019-06-26, 最終更新日: 2024-03-20)

主引用文献

Jung, J.,Grant, T.,Thomas, D.R.,Diehnelt, C.W.,Grigorieff, N.,Joshua-Tor, L.
High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations.
Proc.Natl.Acad.Sci.USA, 116:12828-12832, 2019

PubMed Abstract: Noroviruses are a leading cause of foodborne illnesses worldwide. Although GII.4 strains have been responsible for most norovirus outbreaks, the assembled virus shell structures have been available in detail for only a single strain (GI.1). We present high-resolution (2.6- to 4.1-Å) cryoelectron microscopy (cryo-EM) structures of GII.4, GII.2, GI.7, and GI.1 human norovirus outbreak strain virus-like particles (VLPs). Although norovirus VLPs have been thought to exist in a single-sized assembly, our structures reveal polymorphism between and within genogroups, with small, medium, and large particle sizes observed. Using asymmetric reconstruction, we were able to resolve a Zn metal ion adjacent to the coreceptor binding site, which affected the structural stability of the shell. Our structures serve as valuable templates for facilitating vaccine formulations.

PubMed: 31182604
DOI: 10.1073/pnas.1903562116

実験手法

ELECTRON MICROSCOPY (2.6 Å)