7EQ4

Crystal Structure of the N-terminus of Nonstructural protein 1 from SARS-CoV-2

Summary for 7EQ4

• Entry DOI: 10.2210/pdb7eq4/pdb
• Descriptor: Host translation inhibitor nsp1 (2 entities in total)
• Functional Keywords: sars-cov-2, nsp1, protein translation, ribosome, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 1
• Total formula weight: 13852.98

Authors

Liu, Y.,Ke, Z.,Hu, H.,Zhao, K.,Xiao, J.,Xia, Y.,Li, Y. (deposition date: 2021-04-29, release date: 2021-06-09, Last modification date: 2023-11-29)

Primary citation

Zhao, K.,Ke, Z.,Hu, H.,Liu, Y.,Li, A.,Hua, R.,Guo, F.,Xiao, J.,Zhang, Y.,Duan, L.,Yan, X.F.,Gao, Y.G.,Liu, B.,Xia, Y.,Li, Y.
Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstructural Protein 1.
Microbiol Spectr, 9:e0016921-e0016921, 2021

PubMed Abstract: Nonstructural protein 1 (Nsp1) of severe acute respiratory syndrome coronaviruses (SARS-CoVs) is an important pathogenic factor that inhibits host protein translation by means of its C terminus. However, its N-terminal function remains elusive. Here, we determined the crystal structure of the N terminus (amino acids [aa] 11 to 125) of SARS-CoV-2 Nsp1 at a 1.25-Å resolution. Further functional assays showed that the N terminus of SARS-CoVs Nsp1 alone loses the ability to colocalize with ribosomes and inhibit protein translation. The C terminus of Nsp1 can colocalize with ribosomes, but its protein translation inhibition ability is significantly weakened. Interestingly, fusing the C terminus of Nsp1 with enhanced green fluorescent protein (EGFP) or other proteins in place of its N terminus restored the protein translation inhibitory ability to a level equivalent to that of full-length Nsp1. Thus, our results suggest that the N terminus of Nsp1 is able to stabilize the binding of the Nsp1 C terminus to ribosomes and act as a nonspecific barrier to block the mRNA channel, thus abrogating host mRNA translation.

PubMed: 34132580
DOI: 10.1128/Spectrum.00169-21

Experimental method

X-RAY DIFFRACTION (1.25 Å)