EMD-25984

Single-particle
3.5 Å
EMD-25984 Deposition: 18/01/2022
Map released: 23/02/2022
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-25984

SARS-CoV-2 Omicron 1-RBD up Spike Protein Trimer without the P986-P987 stabilizing mutations (S-GSAS-Omicron)

EMD-25984

Single-particle
3.5 Å
EMD-25984 Deposition: 18/01/2022
Map released: 23/02/2022
Last modified: 06/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Severe acute respiratory syndrome coronavirus 2
Sample: SARS-CoV-2 S-GSAS-Omicron Spike Ectodomain
Fitted models: 7tl9 (Avg. Q-score: 0.411)

Deposition Authors: Stalls V, Acharya P
Structural diversity of the SARS-CoV-2 Omicron spike.
PUBMED: 35447081
DOI: doi:10.1016/j.molcel.2022.03.028
ISSN: 1097-2765
ASTM: MOCEFL
Abstract:
Aided by extensive spike protein mutation, the SARS-CoV-2 Omicron variant overtook the previously dominant Delta variant. Spike conformation plays an essential role in SARS-CoV-2 evolution via changes in receptor-binding domain (RBD) and neutralizing antibody epitope presentation, affecting virus transmissibility and immune evasion. Here, we determine cryo-EM structures of the Omicron and Delta spikes to understand the conformational impacts of mutations in each. The Omicron spike structure revealed an unusually tightly packed RBD organization with long range impacts that were not observed in the Delta spike. Binding and crystallography revealed increased flexibility at the functionally critical fusion peptide site in the Omicron spike. These results reveal a highly evolved Omicron spike architecture with possible impacts on its high levels of immune evasion and transmissibility.