Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9.
journal contributionposted on 30.09.2021, 11:50 by Erika F Dudás, Rita Puglisi, Sophie Marianne Korn, Caterina Alfano, Maria Laura Bellone, Fabrizio Dal Piaz, Geoff Kelly, Elisa Monaca, Andreas Schlundt, Harald Schwalbe, Annalisa Pastore
As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.