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

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 () and Ervin Fodor ()
Additional contact information
Narin Hengrung: Sir William Dunn School of Pathology, 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
Jonathan M. Grimes: Henry Wellcome Building for Genomic Medicine, University of Oxford
Ervin Fodor: Sir William Dunn School of Pathology, University of Oxford

Nature, 2015, vol. 527, issue 7576, 114-117

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.

Date: 2015
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DOI: 10.1038/nature15525

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