7E9T

Nanometer resolution in situ structure of SARS-CoV-2 post-fusion spike

Summary for 7E9T

• Entry DOI: 10.2210/pdb7e9t/pdb
• EMDB information: 31037
• Descriptor: Spike protein S2, 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, ... (4 entities in total)
• Functional Keywords: sars-cov-2, in situ, post-fusion, spike, cryo-sta, virus
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 3
• Total formula weight: 184560.50

Authors

Zhu, Y.,Tai, L.,Zhu, G.,Yin, G.,Sun, F. (deposition date: 2021-03-05, release date: 2021-11-17, Last modification date: 2024-10-16)

Primary citation

Tai, L.,Zhu, G.,Yang, M.,Cao, L.,Xing, X.,Yin, G.,Chan, C.,Qin, C.,Rao, Z.,Wang, X.,Sun, F.,Zhu, Y.
Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in β-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.

PubMed: 34782481
DOI: 10.1073/pnas.2112703118

Experimental method

ELECTRON MICROSCOPY (10.9 Å)