7TEI
SARS-CoV-2 Omicron 1-RBD up Spike Protein Trimer without the P986-P987 stabilizing mutations (S-GSAS-Omicron)
This is a non-PDB format compatible entry.
Summary for 7TEI
| Entry DOI | 10.2210/pdb7tei/pdb |
| EMDB information | 25846 |
| Descriptor | Spike glycoprotein, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | omicron spike protein, sars-cov-2, variant of concern, 1-up, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 |
| Total number of polymer chains | 3 |
| Total formula weight | 403930.50 |
| Authors | Stalls, V.,Acharya, P. (deposition date: 2022-01-05, release date: 2022-02-16, Last modification date: 2023-04-12) |
| Primary citation | Gobeil, S.M.,Henderson, R.,Stalls, V.,Janowska, K.,Huang, X.,May, A.,Speakman, M.,Beaudoin, E.,Manne, K.,Li, D.,Parks, R.,Barr, M.,Deyton, M.,Martin, M.,Mansouri, K.,Edwards, R.J.,Eaton, A.,Montefiori, D.C.,Sempowski, G.D.,Saunders, K.O.,Wiehe, K.,Williams, W.,Korber, B.,Haynes, B.F.,Acharya, P. Structural diversity of the SARS-CoV-2 Omicron spike. Mol.Cell, 82:2050-2068.e6, 2022 Cited by PubMed 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. PubMed: 35447081DOI: 10.1016/j.molcel.2022.03.028 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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