7MY8
Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles
Summary for 7MY8
| Entry DOI | 10.2210/pdb7my8/pdb |
| NMR Information | BMRB: 30909 |
| Descriptor | Spike protein S2 (1 entity in total) |
| Functional Keywords | fusion peptide, lipid binding protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
| Total number of polymer chains | 1 |
| Total formula weight | 4585.22 |
| Authors | Koppisetti, R.K.,Fulcher, Y.G.,Van Doren, S.R. (deposition date: 2021-05-20, release date: 2021-08-18, Last modification date: 2024-10-23) |
| Primary citation | Koppisetti, R.K.,Fulcher, Y.G.,Van Doren, S.R. Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles. J.Am.Chem.Soc., 143:13205-13211, 2021 Cited by PubMed Abstract: The receptor binding and proteolysis of Spike of SARS-CoV-2 release its S subunit to rearrange and catalyze viral-cell fusion. This deploys the fusion peptide for insertion into the cell membranes targeted. We show that this fusion peptide transforms from intrinsic disorder in solution into a wedge-shaped structure inserted in bilayered micelles, according to chemical shifts, N NMR relaxation, and NOEs. The globular fold of three helices contrasts the open, extended forms of this region observed in the electron density of compact prefusion states. In the hydrophobic, narrow end of the wedge, helices 1 and 2 contact the fatty acyl chains of phospholipids, according to NOEs and proximity to a nitroxide spin label deep in the membrane mimic. The polar end of the wedge may engage and displace lipid head groups and bind Ca ions for membrane fusion. Polar helix 3 protrudes from the bilayer where it might be accessible to antibodies. PubMed: 34375093DOI: 10.1021/jacs.1c05435 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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