6NUS

SARS-Coronavirus NSP12 bound to NSP8 co-factor

6NUS の概要

• エントリーDOI: 10.2210/pdb6nus/pdb
• EMDBエントリー: 0520 0521
• 分子名称: NSP12, NSP8, ZINC ION (3 entities in total)
• 機能のキーワード: coronavirus, polymerase, non-structural protein, viral protein
• 由来する生物種: Human SARS coronavirus (SARS-CoV); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 131295.84

構造登録者

Kirchdoerfer, R.N.,Ward, A.B. (登録日: 2019-02-01, 公開日: 2019-05-29, 最終更新日: 2024-03-20)

主引用文献

Kirchdoerfer, R.N.,Ward, A.B.
Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors.
Nat Commun, 10:2342-2342, 2019

PubMed Abstract: Recent history is punctuated by the emergence of highly pathogenic coronaviruses such as SARS- and MERS-CoV into human circulation. Upon infecting host cells, coronaviruses assemble a multi-subunit RNA-synthesis complex of viral non-structural proteins (nsp) responsible for the replication and transcription of the viral genome. Here, we present the 3.1 Å resolution structure of the SARS-CoV nsp12 polymerase bound to its essential co-factors, nsp7 and nsp8, using single particle cryo-electron microscopy. nsp12 possesses an architecture common to all viral polymerases as well as a large N-terminal extension containing a kinase-like fold and is bound by two nsp8 co-factors. This structure illuminates the assembly of the coronavirus core RNA-synthesis machinery, provides key insights into nsp12 polymerase catalysis and fidelity and acts as a template for the design of novel antiviral therapeutics.

PubMed: 31138817
DOI: 10.1038/s41467-019-10280-3

実験手法

ELECTRON MICROSCOPY (3.5 Å)