Asset Details
Do you wish to reserve the book?
Structure of replicating SARS-CoV-2 polymerase
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structure of replicating SARS-CoV-2 polymerase
Do you wish to request the book?
Structure of replicating SARS-CoV-2 polymerase
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structure of replicating SARS-CoV-2 polymerase
2020
Overview
The new coronavirus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) uses an RNA-dependent RNA polymerase (RdRp) for the replication of its genome and the transcription of its genes
1
–
3
. Here we present a cryo-electron microscopy structure of the SARS-CoV-2 RdRp in an active form that mimics the replicating enzyme. The structure comprises the viral proteins non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template–product duplex. The active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity with conserved residues. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged ‘sliding poles’. These sliding poles can account for the known processivity of RdRp that is required for replicating the long genome of coronaviruses
3
. Our results enable a detailed analysis of the inhibitory mechanisms that underlie the antiviral activity of substances such as remdesivir, a drug for the treatment of coronavirus disease 2019 (COVID-19)
4
.
A cryo-electron microscopy structure of the RNA-dependent RNA polymerase of SARS-CoV-2 sheds light on coronavirus replication and enables the analysis of the inhibitory mechanisms of candidate antiviral drugs.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Adenosine Monophosphate - analogs & derivatives
/ Adenosine Monophosphate - pharmacology
/ Alanine - analogs & derivatives
/ Betacoronavirus - drug effects
/ Betacoronavirus - enzymology
/ Betacoronavirus - ultrastructure
/ Cloning
/ Coronavirus RNA-Dependent RNA Polymerase
/ COVID-19
/ Enzymes
/ Genes
/ Genomes
/ Humanities and Social Sciences
/ Poles
/ Proteins
/ RNA-Dependent RNA Polymerase - chemistry
/ RNA-Dependent RNA Polymerase - genetics
/ RNA-Dependent RNA Polymerase - metabolism
/ RNA-Dependent RNA Polymerase - ultrastructure
/ Science
/ Severe acute respiratory syndrome coronavirus 2
/ Sliding
/ Viral Nonstructural Proteins - chemistry
/ Viral Nonstructural Proteins - genetics
