MersV1, PubMed, Corpus, bibRecord, 000521

Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors.

Identifieur interne : 000521 ( PubMed/Corpus ); précédent : 000520; suivant : 000522

Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors.

Auteurs : Robert N. Kirchdoerfer ; Andrew B. Ward

Source :

Nature communications [ 2041-1723 ] ; 2019.

RBID : pubmed:31138817

English descriptors

KwdEn :
- Coenzymes (ultrastructure), Cryoelectron Microscopy, DNA-Directed RNA Polymerases (ultrastructure), Genome, Viral, SARS Virus (metabolism), SARS Virus (ultrastructure), Viral Nonstructural Proteins (ultrastructure).
MESH :
- chemical , ultrastructure : Coenzymes, DNA-Directed RNA Polymerases, Viral Nonstructural Proteins.
- metabolism : SARS Virus.
- ultrastructure : SARS Virus.
- Cryoelectron Microscopy, Genome, Viral.

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.

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

Links to Exploration step

pubmed:31138817

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    PubMed
   |étape=   Corpus
   |type=    RBID
   |clé=     pubmed:31138817
   |texte=   Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors.
}}

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	Serveur d'exploration MERS
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Serveur d'exploration MERS

Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors.

Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors.

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