X-ray structure and activities of an essential Mononegavirales L-protein domain - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2015

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

Résumé

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 (SAMP) also contains a novel pocket (NSP) that can accommodate a nucleoside. CR-VI lacks an obvious cap-binding site, and the SAMP-adjoining site holding the nucleotides undergoing methylation (SUBP) 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.
Fichier principal
Vignette du fichier
ncomms9749.pdf (1.99 Mo) Télécharger le fichier
Origine Fichiers éditeurs autorisés sur une archive ouverte
Loading...

Dates et versions

hal-01439027 , version 1 (07-01-2020)

Licence

Identifiants

Citer

Guido C. Paesen, Axelle Collet, Corinne Sallamand, Francoise Debart, Jean-Jacques Vasseur, et al.. X-ray structure and activities of an essential Mononegavirales L-protein domain. Nature Communications, 2015, 6, pp.8749. ⟨10.1038/ncomms9749⟩. ⟨hal-01439027⟩
70 Consultations
187 Téléchargements

Altmetric

Partager

Gmail Mastodon Facebook X LinkedIn More