7K3N

Crystal Structure of NSP1 from SARS-CoV-2

Summary for 7K3N

• Entry DOI: 10.2210/pdb7k3n/pdb
• Descriptor: Host translation inhibitor nsp1 (2 entities in total)
• Functional Keywords: sars-cov2, nsp1, non-structural protein 1, covid19, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 1
• Total formula weight: 19801.29

Authors

Semper, C.,Watanabe, N.,Chang, C.,Savchenko, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2020-09-11, release date: 2020-09-30, Last modification date: 2023-10-18)

Primary citation

Semper, C.,Watanabe, N.,Savchenko, A.
Structural characterization of nonstructural protein 1 from SARS-CoV-2.
Iscience, 24:101903-101903, 2021

PubMed Abstract: Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a single-stranded, enveloped RNA virus and the etiological agent of the current coronavirus disease 2019 pandemic. Efficient replication of the virus relies on the activity of nonstructural protein 1 (Nsp1), a major virulence factor shown to facilitate suppression of host gene expression through promotion of host mRNA degradation and interaction with the 40S ribosomal subunit. Here, we report the crystal structure of the globular domain of SARS-CoV-2 Nsp1, encompassing residues 13 to 127, at a resolution of 1.65 Å. Our structure features a six-stranded, capped β-barrel motif similar to Nsp1 from SARS-CoV and reveals how variations in amino acid sequence manifest as distinct structural features. Combining our high-resolution crystal structure with existing data on the C-terminus of Nsp1 from SARS-CoV-2, we propose a model of the full-length protein. Our results provide insight into the molecular structure of a major pathogenic determinant of SARS-CoV-2.

PubMed: 33319167
DOI: 10.1016/j.isci.2020.101903

Experimental method

X-RAY DIFFRACTION (1.65 Å)