8ENY
Crystal structure of alpha-COPI-WD40 domain R13A mutant.
Summary for 8ENY
| Entry DOI | 10.2210/pdb8eny/pdb |
| Descriptor | Putative coatomer subunit alpha, ACETYL GROUP (3 entities in total) |
| Functional Keywords | copi, protein trafficking, sars-cov-2 spike, dibasic motif, protein transport |
| Biological source | Schizosaccharomyces pombe (fission yeast) |
| Total number of polymer chains | 3 |
| Total formula weight | 116490.68 |
| Authors | |
| Primary citation | Dey, D.,Qing, E.,He, Y.,Chen, Y.,Jennings, B.,Cohn, W.,Singh, S.,Gakhar, L.,Schnicker, N.J.,Pierce, B.G.,Whitelegge, J.P.,Doray, B.,Orban, J.,Gallagher, T.,Hasan, S.S. A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs. Nat Commun, 14:8358-8358, 2023 Cited by PubMed Abstract: The spike (S) protein of SARS-CoV-2 is delivered to the virion assembly site in the ER-Golgi Intermediate Compartment (ERGIC) from both the ER and cis-Golgi in infected cells. However, the relevance and modulatory mechanism of this bidirectional trafficking are unclear. Here, using structure-function analyses, we show that S incorporation into virus-like particles (VLP) and VLP fusogenicity are determined by coatomer-dependent S delivery from the cis-Golgi and restricted by S-coatomer dissociation. Although S mimicry of the host coatomer-binding dibasic motif ensures retrograde trafficking to the ERGIC, avoidance of the host-like C-terminal acidic residue is critical for S-coatomer dissociation and therefore incorporation into virions or export for cell-cell fusion. Because this C-terminal residue is the key determinant of SARS-CoV-2 assembly and fusogenicity, our work provides a framework for the export of S protein encoded in genetic vaccines for surface display and immune activation. PubMed: 38102143DOI: 10.1038/s41467-023-44076-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
