8FDW
Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane
Summary for 8FDW
Entry DOI | 10.2210/pdb8fdw/pdb |
EMDB information | 29016 |
Descriptor | Spike protein S2, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
Functional Keywords | viral protein |
Biological source | Severe acute respiratory syndrome coronavirus |
Total number of polymer chains | 3 |
Total formula weight | 215858.03 |
Authors | Zhang, J.,Shi, W.,Cai, Y.F.,Zhu, H.S.,Peng, H.Q.,Voyer, J.,Volloch, S.R.,Cao, H.,Mayer, M.L.,Song, K.K.,Xu, C.,Lu, J.M.,Chen, B. (deposition date: 2022-12-05, release date: 2023-05-10, Last modification date: 2024-11-06) |
Primary citation | Shi, W.,Cai, Y.,Zhu, H.,Peng, H.,Voyer, J.,Rits-Volloch, S.,Cao, H.,Mayer, M.L.,Song, K.,Xu, C.,Lu, J.,Zhang, J.,Chen, B. Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane. Nature, 619:403-409, 2023 Cited by PubMed Abstract: The entry of SARS-CoV-2 into host cells depends on the refolding of the virus-encoded spike protein from a prefusion conformation, which is metastable after cleavage, to a lower-energy stable postfusion conformation. This transition overcomes kinetic barriers for fusion of viral and target cell membranes. Here we report a cryogenic electron microscopy (cryo-EM) structure of the intact postfusion spike in a lipid bilayer that represents the single-membrane product of the fusion reaction. The structure provides structural definition of the functionally critical membrane-interacting segments, including the fusion peptide and transmembrane anchor. The internal fusion peptide forms a hairpin-like wedge that spans almost the entire lipid bilayer and the transmembrane segment wraps around the fusion peptide at the last stage of membrane fusion. These results advance our understanding of the spike protein in a membrane environment and may guide development of intervention strategies. PubMed: 37285872DOI: 10.1038/s41586-023-06273-4 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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