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Crystal structure of the RNA-dependent RNA polymerase from influenza C virus

Author

Listed:
  • Narin Hengrung

    (Sir William Dunn School of Pathology, University of Oxford
    Henry Wellcome Building for Genomic Medicine, University of Oxford)

  • Kamel El Omari

    (Henry Wellcome Building for Genomic Medicine, University of Oxford)

  • Itziar Serna Martin

    (Sir William Dunn School of Pathology, University of Oxford)

  • Frank T. Vreede

    (Sir William Dunn School of Pathology, University of Oxford)

  • Stephen Cusack

    (European Molecular Biology Laboratory, Grenoble Outstation and University Grenoble Alpes-Centre National de la Recherche Scientifique-EMBL Unit of Virus Host-Cell Interactions)

  • Robert P. Rambo

    (Diamond Light Source Ltd, Harwell Science & Innovation Campus)

  • Clemens Vonrhein

    (Global Phasing Ltd)

  • Gérard Bricogne

    (Global Phasing Ltd)

  • David I. Stuart

    (Henry Wellcome Building for Genomic Medicine, University of Oxford
    Diamond Light Source Ltd, Harwell Science & Innovation Campus)

  • Jonathan M. Grimes

    (Henry Wellcome Building for Genomic Medicine, University of Oxford
    Diamond Light Source Ltd, Harwell Science & Innovation Campus)

  • Ervin Fodor

    (Sir William Dunn School of Pathology, University of Oxford)

Abstract

The X-ray crystal structure of influenza C virus polymerase, captured in a closed, pre-activation confirmation, is solved at 3.9 Å resolution; comparison with previous RNA-bound structures reveals large conformational changes associated with RNA binding and activation, and illustrates the notable flexibility of the influenza virus RNA polymerase.

Suggested Citation

  • Narin Hengrung & Kamel El Omari & Itziar Serna Martin & Frank T. Vreede & Stephen Cusack & Robert P. Rambo & Clemens Vonrhein & Gérard Bricogne & David I. Stuart & Jonathan M. Grimes & Ervin Fodor, 2015. "Crystal structure of the RNA-dependent RNA polymerase from influenza C virus," Nature, Nature, vol. 527(7576), pages 114-117, November.
    • Handle: RePEc:nat:nature:v:527:y:2015:i:7576:d:10.1038_nature15525
    DOI: 10.1038/nature15525
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    Cited by:

    1. Jeremy R. Keown & Zihan Zhu & Loïc Carrique & Haitian Fan & Alexander P. Walker & Itziar Serna Martin & Els Pardon & Jan Steyaert & Ervin Fodor & Jonathan M. Grimes, 2022. "Mapping inhibitory sites on the RNA polymerase of the 1918 pandemic influenza virus using nanobodies," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Benoît Arragain & Tim Krischuns & Martin Pelosse & Petra Drncova & Martin Blackledge & Nadia Naffakh & Stephen Cusack, 2024. "Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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