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Cryo-EM of SARS-CoV-2 nsp13-replication-transcription complex (nsp13-RTC)

ABSTRACT:

SUBMITTER: Seth A Darst

PROVIDER: EMPIAR-12596 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex.

Chen James J Malone Brandon B Llewellyn Eliza E Grasso Michael M Shelton Patrick M M PMM Olinares Paul Dominic B PDB Maruthi Kashyap K Eng Edward T ET Vatandaslar Hasan H Chait Brian T BT Kapoor Tarun M TM Darst Seth A SA Campbell Elizabeth A EA

Cell 20200728 6

SARS-CoV-2 is the causative agent of the 2019-2020 pandemic. The SARS-CoV-2 genome is replicated and transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp8<sub>2</sub>/nsp12) along with a cast of accessory factors. One of these factors is the nsp13 helicase. Both the holo-RdRp and nsp13 are essential for viral replication and are targets for treating the disease COVID-19. Here we present cryoelectron microscopic structures of the SARS-CoV-2 holo-RdRp with an RNA template ...[more]

PMID: 32783916

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Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex.

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Cryo-EM Structure of an Extended SARS-CoV-2 Replication and Transcription Complex Reveals an Intermediate State in Cap Synthesis.

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Architecture of a SARS-CoV-2 mini replication and transcription complex.

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