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DOI | 10.2210/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: 31182604DOI: 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
検証レポート(詳細版)をダウンロード