6ZOY
Structure of Disulphide-stabilized SARS-CoV-2 Spike Protein Trimer (x1 disulphide-bond mutant, S383C, D985C, K986P, V987P, single Arg S1/S2 cleavage site) in Closed State
Summary for 6ZOY
| Entry DOI | 10.2210/pdb6zoy/pdb |
| EMDB information | 11330 |
| 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 | coronavirus, sars-cov-2, spike protein, s protein, s antigen, covid-19, receptor binding, membrane fusion, vaccine design, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 427905.11 |
| Authors | Xiong, X.,Qu, K.,Scheres, S.H.W.,Briggs, J.A.G. (deposition date: 2020-07-08, release date: 2020-07-22, Last modification date: 2024-10-16) |
| Primary citation | Xiong, X.,Qu, K.,Ciazynska, K.A.,Hosmillo, M.,Carter, A.P.,Ebrahimi, S.,Ke, Z.,Scheres, S.H.W.,Bergamaschi, L.,Grice, G.L.,Zhang, Y.,Nathan, J.A.,Baker, S.,James, L.C.,Baxendale, H.E.,Goodfellow, I.,Doffinger, R.,Briggs, J.A.G. A thermostable, closed SARS-CoV-2 spike protein trimer. Nat.Struct.Mol.Biol., 27:934-941, 2020 Cited by PubMed Abstract: The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. It exhibits substantial conformational flexibility. It transitions from closed to open conformations to expose its receptor-binding site and, subsequently, from prefusion to postfusion conformations to mediate fusion of viral and cellular membranes. S-protein derivatives are components of vaccine candidates and diagnostic assays, as well as tools for research into the biology and immunology of SARS-CoV-2. Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state. Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer. We demonstrate that the designed, thermostable, closed S trimer can be used in serological assays. This protein has potential applications as a reagent for serology, virology and as an immunogen. PubMed: 32737467DOI: 10.1038/s41594-020-0478-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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