Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus

Science

Volumn 326, Issue 5957, 2009, Pages 1279-1283

  Tawar, Rajiv G ^a   Duquerroy, Stéphane ^a,b   Vonrhein, Clemens ^c   Varela, Paloma F ^a,f   Damier Piolle, Laurence ^a   Castagne, Nathalie ^d   MacLellan, Kirsty ^e,g   Bedouelle, Hugues ^a   Bricogne, Gérard ^c   Bhella, David ^e   Eléouët, Jean François ^d   Rey, Félix A ^a  

^a CNRS   (France)

^b UNIVERSITÉ PARIS SACLAY   (France)

^c Global Phasing   (United Kingdom)

^d INRA Institut National de la Recherche Agronomique   (France)

^e UNIVERSITY OF GLASGOW   (United Kingdom)

^f SYNCHROTRON SOLEIL   (France)

^g NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE ALPHA; NUCLEOTIDE; VIRUS NUCLEOPROTEIN; VIRUS RNA;

CRYSTAL STRUCTURE; DISEASE TREATMENT; DRUG DEVELOPMENT; ELECTRON MICROSCOPY; ENZYME ACTIVITY; PATHOGEN; PROTEIN; PUBLIC HEALTH; RESPIRATORY DISEASE; RNA; VACCINE; VIRUS;

ARTICLE; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RESPIRATORY SYNCYTIAL PNEUMOVIRUS; RNA SYNTHESIS; VIRUS NUCLEOCAPSID; VIRUS REPLICATION;

AMINO ACID SEQUENCE; BINDING SITES; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; IMAGE PROCESSING, COMPUTER-ASSISTED; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; NUCLEOCAPSID PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RESPIRATORY SYNCYTIAL VIRUSES; RNA, VIRAL;

RESPIRATORY SYNCYTIAL VIRUS; RICE STRIPE VIRUS; RNA VIRUSES;

EID: 70849108252     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1177634     Document Type: Article

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23. This work was initiated as part of the sixth European Union Framework Programme consortium (http://cordis. europa.eu/life/src/control/qlk2-ct-2001- 01225.htm). We thank A. Albertini, J. Bernard, D. Gerlier, A. Haouz, J. Lepault, M. Moudj'ou, C. Schulze-Briese, E. Stura, P. Weber, and R.P. Yeo for help and/or discussion; M. Backovic, D. Kolakovsky, J. Melero, L. Roux, and A. Tortorici for comments on the manuscript. Diffraction data collection was done at beamline X06SA of the Swiss Light Source and ID23-2 of the European Synchrotron Radiation Facility. R.G.T. benefits from a Marie-Curie RTN fellowship (consortium MRTN-CT-2006-035599, acronym EIHCV). This work was also supported by the French Fondation pour la Recherche Médicale (postdoctoral fellowship to P.F.V.), by a grant from the French Agence Nationale pour la Recherche (Programme MIME) to F.A.R., and by Merck-Serono. The coordinates and structure factors of the N-RNA rings were deposited in the Protein Data Bank with accession number 2wj8. The 3D EM reconstruction was deposited in the Electron Microscopy Data Bank with accession code EMD-1622.