About: X-ray structure and activities of an essential Mononegavirales L-protein domain

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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
title	X-ray structure and activities of an essential Mononegavirales L-protein domain
Creator	Canard, Bruno Decroly, Etienne Vasseur, Jean-Jacques Collet, Axelle Sallamand, Corinne Debart, Franc¸oise Grimes, Jonathan Paesen, Guido
topic	covid:51cf7d2eb2b034eb720e300ec7c185bfe1f69b07#this
source	Medline; PMC
abstract	The L protein of mononegaviruses harbours all catalytic activities for genome replication and transcription. It contains six conserved domains (CR-I to -VI; Fig. 1a). CR-III has been linked to polymerase and polyadenylation activity, CR-V to mRNA capping and CR-VI to cap methylation. However, how these activities are choreographed is poorly understood. Here we present the 2.2-Å X-ray structure and activities of CR-VI+, a portion of human Metapneumovirus L consisting of CR-VI and the poorly conserved region at its C terminus, the +domain. The CR-VI domain has a methyltransferase fold, which besides the typical S-adenosylmethionine-binding site ((SAM)P) also contains a novel pocket ((NS)P) that can accommodate a nucleoside. CR-VI lacks an obvious cap-binding site, and the (SAM)P-adjoining site holding the nucleotides undergoing methylation ((SUB)P) is unusually narrow because of the overhanging +domain. CR-VI+ sequentially methylates caps at their 2′O and N7 positions, and also displays nucleotide triphosphatase activity.
has issue date	2015-11-09(xsd:dateTime)
bibo:doi	10.1038/ncomms9749
bibo:pmid	26549102
has license	cc-by
sha1sum (hex)	51cf7d2eb2b034eb720e300ec7c185bfe1f69b07
schema:url	https://doi.org/10.1038/ncomms9749
resource representing a document's title	X-ray structure and activities of an essential Mononegavirales L-protein domain
has PubMed Central identifier	PMC4659945
has PubMed identifier	26549102
schema:publication	Nat Commun
resource representing a document's body	covid:51cf7d2eb2b034eb720e300ec7c185bfe1f69b07#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/51cf7d2eb2b034eb720e300ec7c185bfe1f69b07
is schema:about of	named entity 'site' named entity 'catalytic' named entity 'domain' named entity 'choreographed' named entity 'site' named entity 'CR-VI' named entity 'CR-V' named entity 'methyltransferase' named entity 'SAM' named entity '2.2' named entity 'phosphonate' named entity 'hydrogen bonded' named entity 'recombinant protein' named entity 'helix' named entity 'Protein' named entity 'single-wavelength anomalous dispersion' named entity 'ligation' named entity 'guanosine' named entity 'virus' named entity 'SARS coronavirus' named entity '1 mM' named entity 'substrates' named entity 'CR-VI' named entity 'activities' named entity 'methylates' named entity 'CR-V' named entity 'nucleotide' named entity '2.2' named entity 'methylation' named entity 'SAM' named entity 'methylation' named entity 'Mononegavirales' named entity 'dot-blot' named entity 'Protein' named entity 'dithiothreitol' named entity 'nuclease' named entity '30 mM' named entity '35°C' named entity 'Thermo Scientific' named entity 'RNA' named entity 'SAM' named entity 'N 1' named entity 'FRET' named entity 'interact' named entity 'transcriptional' named entity 'polymerase' named entity 'motif' named entity 'assay' named entity 'nucleotides' named entity 'virus' named entity 'K-K' named entity 'b-sheet' named entity 'restriction enzymes' named entity 'substrates' named entity 'guanosine' named entity 'New England Biolabs' named entity 'methylated' named entity 'GTP' named entity 'electron density' named entity 'oxygen' named entity 'Cloning' named entity 'precipitation' named entity 'primer' named entity 'K-K' named entity 'transferase' named entity 'methylation' named entity 'flu' named entity 'translocation' named entity 'fetal bovine serum' named entity 'cloned' named entity 'Invitrogen' named entity 'SDS-polyacrylamide gel electrophoresis'

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