Dataset Information
Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN domain
Ontology highlight
ABSTRACT:
SUBMITTER: Elizabeth Campbell
PROVIDER: EMPIAR-11811 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN domain.
Molecular cell 20231026 21
The enzymatic activity of the SARS-CoV-2 nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain is essential for viral propagation, with three distinct activities associated with modification of the nsp9 N terminus, NMPylation, RNAylation, and deRNAylation/capping via a GDP-polyribonucleotidyltransferase reaction. The latter two activities comprise an unconventional mechanism for initiating viral RNA 5' cap formation, while the role of NMPylation is unclear. The structural mechanisms fo ...[more]