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6OTF

Symmetric reconstruction of human norovirus GII.2 Snow Mountain Virus Strain VLP in T=3 symmetry

6OTF の概要
エントリーDOI10.2210/pdb6otf/pdb
EMDBエントリー20195 20197 20198 20199 20201 20202 20205 20206
分子名称Viral protein 1, ZINC ION (2 entities in total)
機能のキーワードcaliciviridae, norovirus, gii.2, snow mountain virus, virus like particle
由来する生物種Snow Mountain virus
タンパク質・核酸の鎖数3
化学式量合計178161.65
構造登録者
Jung, J.,Grant, T.,Thomas, D.R.,Diehnelt, C.W.,Grigorieff, N.,Joshua-Tor, L. (登録日: 2019-05-03, 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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.1 Å)
構造検証レポート
Validation report summary of 6otf
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2024-11-06に公開中

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