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8FDW

Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane

Summary for 8FDW
Entry DOI10.2210/pdb8fdw/pdb
EMDB information29016
DescriptorSpike 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 Keywordsviral protein
Biological sourceSevere acute respiratory syndrome coronavirus
Total number of polymer chains3
Total formula weight215858.03
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 citationShi, 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: 37285872
DOI: 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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