7O35
Crystal Structure of SARS-CoV-2 N-CTD in complex with GTP (I)
Summary for 7O35
| Entry DOI | 10.2210/pdb7o35/pdb |
| Descriptor | Nucleoprotein, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | nucleocapsid, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
| Total number of polymer chains | 4 |
| Total formula weight | 62083.98 |
| Authors | Ciges-Tomas, J.R.,Vilar, M. (deposition date: 2021-04-01, release date: 2022-04-13, Last modification date: 2024-01-31) |
| Primary citation | Rafael Ciges-Tomas, J.,Franco, M.L.,Vilar, M. Identification of a guanine-specific pocket in the protein N of SARS-CoV-2. Commun Biol, 5:711-711, 2022 Cited by PubMed Abstract: The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (N) in open and closed conformations and in complex with guanine triphosphate, GTP. The crystal structure and biochemical studies reveal a specific interaction between the guanine, a nucleotide enriched in the packaging signals regions of coronaviruses, and a highly conserved tryptophan residue (W330). In addition, EMSA assays with SARS-CoV-2 derived RNA hairpin loops from a putative viral packaging sequence showed the preference interaction of the N-CTD to RNA oligonucleotides containing G and the loss of the specificity in the mutant W330A. Here we propose that this interaction may facilitate the viral assembly process. In summary, we have identified a specific guanine-binding pocket in the N protein that may be used to design viral assembly inhibitors. PubMed: 35842466DOI: 10.1038/s42003-022-03647-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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