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

Author

Listed:
  • 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
    Diamond Light Source Limited, Harwell Science and Innovation Campus)

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.

Suggested Citation

  • Guido C. Paesen & Axelle Collet & Corinne Sallamand & Françoise Debart & Jean-Jacques Vasseur & Bruno Canard & Etienne Decroly & Jonathan M. Grimes, 2015. "X-ray structure and activities of an essential Mononegavirales L-protein domain," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9749
    DOI: 10.1038/ncomms9749
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    Cited by:

    1. Qi Peng & Yingying Dong & Mingzhu Jia & Qiannv Liu & Yuhai Bi & Jianxun Qi & Yi Shi, 2024. "Cryo-EM structure of Nipah virus L-P polymerase complex," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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