6ZWV
Cryo-EM structure of SARS-CoV-2 Spike Proteins on intact virions: 3 Closed RBDs
This is a non-PDB format compatible entry.
Summary for 6ZWV
| Entry DOI | 10.2210/pdb6zwv/pdb |
| Related | 6ZWV |
| EMDB information | 11493 11494 11495 11496 11497 11498 |
| Descriptor | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | sars-cov-2, spike protein, virions, glycoprotein, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 437384.05 |
| Authors | Ke, Z.,Qu, K.,Nakane, T.,Xiong, X.,Cortese, M.,Zila, V.,Scheres, S.H.W.,Briggs, J.A.G. (deposition date: 2020-07-28, release date: 2020-08-05, Last modification date: 2024-10-23) |
| Primary citation | Ke, Z.,Oton, J.,Qu, K.,Cortese, M.,Zila, V.,McKeane, L.,Nakane, T.,Zivanov, J.,Neufeldt, C.J.,Cerikan, B.,Lu, J.M.,Peukes, J.,Xiong, X.,Krausslich, H.G.,Scheres, S.H.W.,Bartenschlager, R.,Briggs, J.A.G. Structures and distributions of SARS-CoV-2 spike proteins on intact virions. Nature, 588:498-502, 2020 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. PubMed: 32805734DOI: 10.1038/s41586-020-2665-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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