About: Structural basis of RNA cap modification by SARS-CoV-2

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About: Structural basis of RNA cap modification by SARS-CoV-2 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural basis of RNA cap modification by SARS-CoV-2
Creator	Park, Jun-Gyu Martinez-Sobrido, Luis Arya, Shailee Chan, Siu-Hong Dai, Nan Gupta, Yogesh Hromas, Robert Oladunni, Fatai Qi, Shan Viswanathan, Thiruselvam Kovalskyy, Dmytro Misra, Anurag
Source	Medline; PMC
abstract	The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 illness, has caused millions of infections worldwide. In SARS coronaviruses, the non-structural protein 16 (nsp16), in conjunction with nsp10, methylates the 5′-end of virally encoded mRNAs to mimic cellular mRNAs, thus protecting the virus from host innate immune restriction. We report here the high-resolution structure of a ternary complex of SARS-CoV-2 nsp16 and nsp10 in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine (SAM). The nsp16/nsp10 heterodimer is captured in the act of 2′-O methylation of the ribose sugar of the first nucleotide of SARS-CoV-2 mRNA. We observe large conformational changes associated with substrate binding as the enzyme transitions from a binary to a ternary state. This induced fit model provides mechanistic insights into the 2′-O methylation of the viral mRNA cap. We also discover a distant (25 Å) ligand-binding site unique to SARS-CoV-2, which can alternatively be targeted, in addition to RNA cap and SAM pockets, for antiviral development.
has issue date	2020-07-24(xsd:dateTime)
bibo:doi	10.1038/s41467-020-17496-8
bibo:pmid	32709886
has license	cc-by
sha1sum (hex)	4b127b5d5965d4492d91663352c5220a0ff59157
schema:url	https://doi.org/10.1038/s41467-020-17496-8
resource representing a document's title	Structural basis of RNA cap modification by SARS-CoV-2
has PubMed Central identifier	PMC7381649
has PubMed identifier	32709886
schema:publication	Nat Commun
resource representing a document's body	covid:4b127b5d5965d4492d91663352c5220a0ff59157#body_text
is schema:about of	named entity 'site' named entity 'model' named entity 'mechanistic' named entity 'SARS-CoV-2' named entity 'cognate' covid:arg/4b127b5d5965d4492d91663352c5220a0ff59157 named entity 'This' named entity 'SARS-CoV-2' named entity 'alternatively' named entity 'insights' named entity 'analogue' named entity 'infections' named entity 'heterodimer' named entity 'binary' named entity 'SARS-CoV-2' named entity 'nucleotide' named entity 'cognate' named entity 'SARS' named entity 'induced fit model' named entity 'ternary complex' named entity 'substrate' named entity 'SAM' named entity 'SARS-CoV-2' named entity 'mRNAs' named entity 'mRNAs' named entity 'discover' named entity 'SAM' named entity 'nucleic acids' named entity 'sulfur' named entity 'coronavirus' named entity 'immune response' named entity 'methyl group' named entity 'SAM' named entity 'SARS-CoV-1' named entity 'sugar' named entity 'coronavirus' named entity 'Vaccinia' named entity 'Nature Research' named entity 'adenine' named entity 'crystallization' named entity 'binding pocket' named entity 'ion' named entity 'SAMand' named entity 'ternary complex' named entity 'phosphates' named entity 'RNA' named entity 'N 1' named entity 'RNA' named entity 'SARS-CoV-2' named entity 'pH 8' named entity 'sterically' named entity 'amino-acid' named entity 'sulfur' named entity 'molecular replacement' named entity 'interferon' named entity 'deprotonated' named entity 'tetrad' named entity 'mother liquor' named entity 'gag-knuckle' named entity 'ligands' named entity 'RNA binding' named entity 'N-terminal' named entity 'ligands' named entity 'SAM' named entity 'protein complex' named entity 'vaccinia virus' named entity 'co-purified' named entity 'centrifugation' named entity 'New York City' named entity 'adenosine'

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