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6ZPE

Nonstructural protein 10 (nsp10) from SARS CoV-2

Summary for 6ZPE
Entry DOI10.2210/pdb6zpe/pdb
DescriptorReplicase polyprotein 1ab, ZINC ION, GLYCEROL, ... (5 entities in total)
Functional Keywordssars cov-2, nonstructural protein, nsp10, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
Total number of polymer chains1
Total formula weight13613.51
Authors
Fisher, S.Z.,Kozielski, F. (deposition date: 2020-07-08, release date: 2020-10-14, Last modification date: 2024-01-31)
Primary citationRogstam, 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: 33036230
DOI: 10.3390/ijms21197375
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.58 Å)
Structure validation

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