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6OTF

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

Summary for 6OTF
Entry DOI10.2210/pdb6otf/pdb
EMDB information20195 20197 20198 20199 20201 20202 20205 20206
DescriptorViral protein 1, ZINC ION (2 entities in total)
Functional Keywordscaliciviridae, norovirus, gii.2, snow mountain virus, virus like particle
Biological sourceSnow Mountain virus
Total number of polymer chains3
Total formula weight178161.65
Authors
Jung, J.,Grant, T.,Thomas, D.R.,Diehnelt, C.W.,Grigorieff, N.,Joshua-Tor, L. (deposition date: 2019-05-03, release date: 2019-06-26, Last modification date: 2024-03-20)
Primary citationJung, 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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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數據於2024-11-06公開中

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