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

Guido C. Paesen, Axelle Collet, Corinne Sallamand, Françoise Debart, Jean-Jacques Vasseur, Bruno Canard, Etienne Decroly () and Jonathan M. Grimes ()
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Guido C. Paesen: Wellcome Trust Centre for Human Genetics
Axelle Collet: AFMB, CNRS, Aix-Marseille University
Corinne Sallamand: IBMM, UMR 5247, CNRS, Université Montpellier, ENSCM
Françoise Debart: IBMM, UMR 5247, CNRS, Université Montpellier, ENSCM
Jean-Jacques Vasseur: IBMM, UMR 5247, CNRS, Université Montpellier, ENSCM
Bruno Canard: AFMB, CNRS, Aix-Marseille University
Etienne Decroly: AFMB, CNRS, Aix-Marseille University
Jonathan M. Grimes: Wellcome Trust Centre for Human Genetics

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: 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 (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.

Date: 2015
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DOI: 10.1038/ncomms9749

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