9PYW
SARS-CoV-2 nsp7, nsp8 and nsp12 bound to a primer-template pair with incorporated ara-UMP
Summary for 9PYW
| Entry DOI | 10.2210/pdb9pyw/pdb |
| Related | 9BLF 9PYZ 9PZ0 |
| EMDB information | 72038 |
| Descriptor | RNA-directed RNA polymerase nsp12, Non-structural protein 8, Non-structural protein 7, ... (7 entities in total) |
| Functional Keywords | rna-dependent rna polymerase (rdrp), viral rna synthesis, arabinose utp, nsp7, nsp8, nsp12, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 6 |
| Total formula weight | 185381.87 |
| Authors | |
| Primary citation | Xiao, Z.,Das, A.,Jain, A.,Anderson, T.K.,Cameron, C.E.,Arnold, J.J.,Dulin, D.,Kirchdoerfer, R.N. The 2'-endo conformation of arabinose-CTP and arabinose-UTP inhibit viral polymerases by inducing long pauses. Biorxiv, 2025 Cited by PubMed Abstract: Key to supporting human health in the face of evolving viruses is the development of novel antiviral drug scaffolds with the potential for broad inhibition of viral families. Nucleoside analogs are a key class of drugs that have demonstrated potential for the inhibition of several viral species. Here, we evaluate arabinose nucleotides (ara-NTP) as inhibitors of the SARS-CoV-2 and poliovirus polymerases using biochemistry, biophysics and structural biology. Ara-NTPs compete poorly with their natural counterparts for incorporation into RNA by viral polymerases. However, upon incorporation, ara-NMPs induce long polymerase pausing in both SARS-CoV-2 and poliovirus polymerase RNA elongation. Our studies suggest that subsequent nucleotide incorporation is inhibited at the catalytic step due to the 2'-endo sugar pucker of the incorporated ara-NMP. PubMed: 40909592DOI: 10.1101/2025.08.26.672356 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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