The structure of a dimeric form of SARS-CoV-2 polymerase View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2021-08-24

AUTHORS

Florian A. Jochheim, Dimitry Tegunov, Hauke S. Hillen, Jana Schmitzová, Goran Kokic, Christian Dienemann, Patrick Cramer

ABSTRACT

The coronavirus SARS-CoV-2 uses an RNA-dependent RNA polymerase (RdRp) to replicate and transcribe its genome. Previous structures of the RdRp revealed a monomeric enzyme composed of the catalytic subunit nsp12, two copies of subunit nsp8, and one copy of subunit nsp7. Here we report an alternative, dimeric form of the enzyme and resolve its structure at 5.5 Å resolution. In this structure, the two RdRps contain only one copy of nsp8 each and dimerize via their nsp7 subunits to adopt an antiparallel arrangement. We speculate that the RdRp dimer facilitates template switching during production of sub-genomic RNAs. More... »

PAGES

999

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-021-02529-9

DOI

http://dx.doi.org/10.1038/s42003-021-02529-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1140614961

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/34429502


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