About: Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex

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About: Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex
Creator	Canard, Bruno Decroly, Etienne Coutard, Bruno Ferron, François Lescar, Julien Bouvet, Mickael Debarnot, Claire Gluais, Laure Imbert, Isabelle Ortiz-Lombardia, Miguel Papageorgiou, Nicolas Sharff, Andrew Rard Bricogne, Gé
source	Medline; PMC
abstract	Cellular and viral S-adenosylmethionine-dependent methyltransferases are involved in many regulated processes such as metabolism, detoxification, signal transduction, chromatin remodeling, nucleic acid processing, and mRNA capping. The Severe Acute Respiratory Syndrome coronavirus nsp16 protein is a S-adenosylmethionine-dependent (nucleoside-2′-O)-methyltransferase only active in the presence of its activating partner nsp10. We report the nsp10/nsp16 complex structure at 2.0 Å resolution, which shows nsp10 bound to nsp16 through a ∼930 Å(2) surface area in nsp10. Functional assays identify key residues involved in nsp10/nsp16 association, and in RNA binding or catalysis, the latter likely through a SN2-like mechanism. We present two other crystal structures, the inhibitor Sinefungin bound in the S-adenosylmethionine binding pocket and the tighter complex nsp10(Y96F)/nsp16, providing the first structural insight into the regulation of RNA capping enzymes in (+)RNA viruses.
has issue date	2011-05-26(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1002059
bibo:pmid	21637813
has license	cc-by
sha1sum (hex)	e65736745475f7a3bab0f310edb593acc50528b7
schema:url	https://doi.org/10.1371/journal.ppat.1002059
resource representing a document's title	Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex
has PubMed Central identifier	PMC3102710
has PubMed identifier	21637813
schema:publication	PLoS Pathog
resource representing a document's body	covid:e65736745475f7a3bab0f310edb593acc50528b7#body_text
is schema:about of	named entity 'processing' named entity 'metabolism' named entity 'RNA' named entity 'protein' named entity 'acid' named entity 'Functional Analysis' named entity 'RNA' named entity 'Structure' named entity 'O-Methyltransferase' named entity 'PLoS' named entity 'S-adenosylmethionine' named entity 'binding pocket' named entity 'SN2' named entity 'identify' named entity 'structural' named entity 'enzymes' named entity 'S-adenosylmethionine' named entity 'SN2' named entity 'protein' named entity 'S-adenosylmethionine' named entity 'Functional Analysis' named entity 'RNA viruses' named entity 'KDKE' named entity 'crystallization' named entity 'nsp5' named entity 'nucleotides' named entity 'water molecules' named entity 'electron density' named entity 'sequence identity' named entity 'IPTG' named entity 'S-adenosylhomocysteine' named entity 'RNA molecule' named entity 'binding site' named entity 'protein' named entity 'RNA' named entity 'nonstructural proteins' named entity 'nucleobase' named entity 'C-terminus' named entity 'wild-type' named entity 'wild-type' named entity 'crystal structure' named entity 'guanine' named entity 'substrates' named entity 'antiviral drug' named entity 'heterodimer' named entity 'hydrogen bonds' named entity 'SART' named entity 'Bluetongue virus' named entity 'C-terminus' named entity 'oligonucleotide' named entity 'conformation' named entity 'capping enzyme' named entity 'GTP' named entity 'dimer' named entity 'Electron density' named entity 'viral RNA' named entity 'mutation' named entity 'RNA' named entity 'diphosphate' named entity 'methyl' named entity 'crystal structure' named entity 'conserved residues' named entity 'adenine' named entity 'RNA' named entity 'chemical reaction' named entity 'binding pocket' named entity 'structure-based drug design' named entity 'phenylalanine' named entity 'S-adenosylmethionine'

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