Journal: Commun Biol / Year: 2021 Title: The structure of a dimeric form of SARS-CoV-2 polymerase. 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 ...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.
History
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Jun 24, 2021
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Header (metadata) release
Aug 25, 2021
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Map release
Aug 25, 2021
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Update
Jul 17, 2024
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Current status
Jul 17, 2024
Processing site: PDBe / Status: Released
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Structure visualization
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EMPIAR-10741 (Title: Single particle cryo-EM dataset of Sars-CoV2 Rna dependent RNA polymerase Data size: 2.7 TB Data #1: Unaligned TIF movies of SARS-CoV2 RdRp in complex with nsp7, nsp8 and RNA [micrographs - multiframe])
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