7KDI
SARS-CoV-2 D614G 3 RBD down Spike Protein Trimer fully cleaved by furin without the P986-P987 stabilizing mutations (S-RRAR-D614G)
Summary for 7KDI
| Entry DOI | 10.2210/pdb7kdi/pdb |
| EMDB information | 22821 22822 22823 22824 22825 22826 |
| 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 trimer, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 441513.27 |
| Authors | Gobeil, S.,Acharya, P. (deposition date: 2020-10-08, release date: 2020-11-04, Last modification date: 2024-11-06) |
| Primary citation | Gobeil, S.M.,Janowska, K.,McDowell, S.,Mansouri, K.,Parks, R.,Manne, K.,Stalls, V.,Kopp, M.F.,Henderson, R.,Edwards, R.J.,Haynes, B.F.,Acharya, P. D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction. Cell Rep, 34:108630-108630, 2021 Cited by PubMed Abstract: The severe acute respiratory coronavirus 2 (SARS-CoV-2) spike (S) protein is the target of vaccine design efforts to end the coronavirus disease 2019 (COVID-19) pandemic. Despite a low mutation rate, isolates with the D614G substitution in the S protein appeared early during the pandemic and are now the dominant form worldwide. Here, we explore S conformational changes and the effects of the D614G mutation on a soluble S ectodomain construct. Cryoelectron microscopy (cryo-EM) structures reveal altered receptor binding domain (RBD) disposition; antigenicity and proteolysis experiments reveal structural changes and enhanced furin cleavage efficiency of the G614 variant. Furthermore, furin cleavage alters the up/down ratio of the RBDs in the G614 S ectodomain, demonstrating an allosteric effect on RBD positioning triggered by changes in the SD2 region, which harbors residue 614 and the furin cleavage site. Our results elucidate SARS-CoV-2 S conformational landscape and allostery and have implications for vaccine design. PubMed: 33417835DOI: 10.1016/j.celrep.2020.108630 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.26 Å) |
Structure validation
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