6ZCT
Nonstructural protein 10 (nsp10) from SARS CoV-2
Summary for 6ZCT
Entry DOI | 10.2210/pdb6zct/pdb |
Descriptor | nsp10, ZINC ION (3 entities in total) |
Functional Keywords | sars cov-2, nonstructural protein, nsp10, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
Total number of polymer chains | 1 |
Total formula weight | 13415.05 |
Authors | Rogstam, A.,Nyblom, M.,Christensen, S.,Sele, C.,Lindvall, T.,Rasmussen, A.A.,Andre, I.,Fisher, S.Z.,Knecht, W.,Kozielski, F. (deposition date: 2020-06-12, release date: 2020-06-24, Last modification date: 2024-01-24) |
Primary citation | Rogstam, A.,Nyblom, M.,Christensen, S.,Sele, C.,Talibov, V.O.,Lindvall, T.,Rasmussen, A.A.,Andre, I.,Fisher, Z.,Knecht, W.,Kozielski, F. Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2. Int J Mol Sci, 21:-, 2020 Cited by PubMed Abstract: Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), causing Coronavirus Disease 19 (COVID-19), emerged at the end of 2019 and quickly spread to cause a global pandemic with severe socio-economic consequences. The early sequencing of its RNA genome revealed its high similarity to SARS, likely to have originated from bats. The SARS-CoV-2 non-structural protein 10 (nsp10) displays high sequence similarity with its SARS homologue, which binds to and stimulates the 3'-to-5' exoribonuclease and the 2'-O-methlytransferase activities of nsps 14 and 16, respectively. Here, we report the biophysical characterization and 1.6 Å resolution structure of the unbound form of nsp10 from SARS-CoV-2 and compare it to the structures of its SARS homologue and the complex-bound form with nsp16 from SARS-CoV-2. The crystal structure and solution behaviour of nsp10 will not only form the basis for understanding the role of SARS-CoV-2 nsp10 as a central player of the viral RNA capping apparatus, but will also serve as a basis for the development of inhibitors of nsp10, interfering with crucial functions of the replication-transcription complex and virus replication. PubMed: 33036230DOI: 10.3390/ijms21197375 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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