6VWW

Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2.

Summary for 6VWW

• Entry DOI: 10.2210/pdb6vww/pdb
• Descriptor: Uridylate-specific endoribonuclease, GLYCEROL, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: sars corona virus, endonuclease, structural genomics, center for structural genomics of infectious diseases, csgid, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 2
• Total formula weight: 84383.24

Authors

Kim, Y.,Jedrzejczak, R.,Maltseva, N.,Endres, M.,Godzik, A.,Michalska, K.,Joachimiak, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2020-02-20, release date: 2020-03-04, Last modification date: 2023-10-11)

Primary citation

Kim, Y.,Jedrzejczak, R.,Maltseva, N.I.,Wilamowski, M.,Endres, M.,Godzik, A.,Michalska, K.,Joachimiak, A.
Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2.
Protein Sci., 29:1596-1605, 2020

PubMed Abstract: Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) is rapidly spreading around the world. There is no existing vaccine or proven drug to prevent infections and stop virus proliferation. Although this virus is similar to human and animal SARS-CoVs and Middle East Respiratory Syndrome coronavirus (MERS-CoVs), the detailed information about SARS-CoV-2 proteins structures and functions is urgently needed to rapidly develop effective vaccines, antibodies, and antivirals. We applied high-throughput protein production and structure determination pipeline at the Center for Structural Genomics of Infectious Diseases to produce SARS-CoV-2 proteins and structures. Here we report two high-resolution crystal structures of endoribonuclease Nsp15/NendoU. We compare these structures with previously reported homologs from SARS and MERS coronaviruses.

PubMed: 32304108
DOI: 10.1002/pro.3873

Experimental method

X-RAY DIFFRACTION (2.2 Å)