6YZ1

The crystal structure of SARS-CoV-2 nsp10-nsp16 methyltransferase complex with Sinefungin

6YZ1 の概要

• エントリーDOI: 10.2210/pdb6yz1/pdb
• 分子名称: nsp16, nsp10, SINEFUNGIN, ... (6 entities in total)
• 機能のキーワード: sars-cov-2, viral replication, coronavirus, methyltransferase, sinefungin, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47319.96

構造登録者

Krafcikova, P.,Silhan, J.,Nencka, R.,Boura, E. (登録日: 2020-05-06, 公開日: 2020-05-13, 最終更新日: 2024-01-24)

主引用文献

Krafcikova, P.,Silhan, J.,Nencka, R.,Boura, E.
Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin.
Nat Commun, 11:3717-3717, 2020

PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the COVID-19 pandemic. 2'-O-RNA methyltransferase (MTase) is one of the enzymes of this virus that is a potential target for antiviral therapy as it is crucial for RNA cap formation; an essential process for viral RNA stability. This MTase function is associated with the nsp16 protein, which requires a cofactor, nsp10, for its proper activity. Here we show the crystal structure of the nsp10-nsp16 complex bound to the pan-MTase inhibitor sinefungin in the active site. Our structural comparisons reveal low conservation of the MTase catalytic site between Zika and SARS-CoV-2 viruses, but high conservation of the MTase active site between SARS-CoV-2 and SARS-CoV viruses; these data suggest that the preparation of MTase inhibitors targeting several coronaviruses - but not flaviviruses - should be feasible. Together, our data add to important information for structure-based drug discovery.

PubMed: 32709887
DOI: 10.1038/s41467-020-17495-9

実験手法

X-RAY DIFFRACTION (2.4 Å)