6ZB5
SARS CoV-2 Spike protein, Closed conformation, C3 symmetry
Summary for 6ZB5
| Entry DOI | 10.2210/pdb6zb5/pdb |
| EMDB information | 11145 |
| 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, ... (4 entities in total) |
| Functional Keywords | sars-cov2, covid, viral protein, linoleic acid, spike |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 425746.46 |
| Authors | Toelzer, C.,Gupta, K.,Yadav, S.K.N.,Burucu, U.,Schaffitzel, C.,Berger, I. (deposition date: 2020-06-07, release date: 2020-09-30, Last modification date: 2020-11-18) |
| Primary citation | Toelzer, C.,Gupta, K.,Yadav, S.K.N.,Borucu, U.,Davidson, A.D.,Kavanagh Williamson, M.,Shoemark, D.K.,Garzoni, F.,Staufer, O.,Milligan, R.,Capin, J.,Mulholland, A.J.,Spatz, J.,Fitzgerald, D.,Berger, I.,Schaffitzel, C. Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein. Science, 370:725-730, 2020 Cited by PubMed Abstract: Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), represents a global crisis. Key to SARS-CoV-2 therapeutic development is unraveling the mechanisms that drive high infectivity, broad tissue tropism, and severe pathology. Our 2.85-angstrom cryo-electron microscopy structure of SARS-CoV-2 spike (S) glycoprotein reveals that the receptor binding domains tightly bind the essential free fatty acid linoleic acid (LA) in three composite binding pockets. A similar pocket also appears to be present in the highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV). LA binding stabilizes a locked S conformation, resulting in reduced angiotensin-converting enzyme 2 (ACE2) interaction in vitro In human cells, LA supplementation synergizes with the COVID-19 drug remdesivir, suppressing SARS-CoV-2 replication. Our structure directly links LA and S, setting the stage for intervention strategies that target LA binding by SARS-CoV-2. PubMed: 32958580DOI: 10.1126/science.abd3255 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.85 Å) |
Structure validation
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