6WXD

SARS-CoV-2 Nsp9 RNA-replicase

Summary for 6WXD

• Entry DOI: 10.2210/pdb6wxd/pdb
• Related: 6w9q
• Descriptor: Non-structural protein 9, SULFATE ION (3 entities in total)
• Functional Keywords: covid-19, sars-cov-2, nsp9, rna replicase, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 2
• Total formula weight: 25492.97

Authors

Littler, D.R.,Gully, B.S.,Riboldi-Tunnicliffe, A.,Rossjohn, J. (deposition date: 2020-05-10, release date: 2020-05-20, Last modification date: 2023-10-18)

Primary citation

Littler, D.R.,Gully, B.S.,Colson, R.N.,Rossjohn, J.
Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9.
Iscience, 23:101258-101258, 2020

PubMed Abstract: Many of the SARS-CoV-2 proteins have related counterparts across the Severe Acute Respiratory Syndrome (SARS-CoV) family. One such protein is non-structural protein 9 (Nsp9), which is thought to mediate viral replication, overall virulence, and viral genomic RNA reproduction. We sought to better characterize the SARS-CoV-2 Nsp9 and subsequently solved its X-ray crystal structure, in an apo form and, unexpectedly, in a peptide-bound form with a sequence originating from a rhinoviral 3C protease sequence (LEVL). The SARS-CoV-2 Nsp9 structure revealed the high level of structural conservation within the Nsp9 family. The exogenous peptide binding site is close to the dimer interface and impacted the relative juxtapositioning of the monomers within the homodimer. We have established a protocol for the production of SARS-CoV-2 Nsp9, determined its structure, and identified a peptide-binding site that warrants further study to understanding Nsp9 function.

PubMed: 32592996
DOI: 10.1016/j.isci.2020.101258

Experimental method

X-RAY DIFFRACTION (2 Å)