The structure of a dimeric form of SARS-CoV-2 polymerase

2021 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​The structure of a dimeric form of SARS-CoV-2 polymerase​
Jochheim, F. A.; Tegunov, D. ; Hillen, H. S. ; Schmitzová, J.; Kokic, G. ; Dienemann, C.   & Cramer, P. ​ (2021) 
Communications Biology4(1) art. 999​.​ DOI: https://doi.org/10.1038/s42003-021-02529-9 

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Authors
Jochheim, Florian A.; Tegunov, Dimitry ; Hillen, Hauke S. ; Schmitzová, Jana; Kokic, Goran ; Dienemann, Christian ; Cramer, Patrick 
Abstract
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.
Issue Date
2021
Journal
Communications Biology 
Project
EXC 2067: Multiscale Bioimaging 
SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente 
FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala 
FOR 2848 | St01: Structure and distribution of ribosomes at the inner mitochondrial membrane 
Working Group
RG Cramer 
RG Hillen (Structure and Function of Molecular Machines) 
eISSN
2399-3642
Language
English

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