2WFS
Fitting of influenza virus NP structure into the 9-fold symmetryzed cryoEM reconstruction of an active RNP particle.
Summary for 2WFS
| Entry DOI | 10.2210/pdb2wfs/pdb |
| EMDB information | 1603 |
| Descriptor | NUCLEOPROTEIN (1 entity in total) |
| Functional Keywords | viral nucleoprotein, host-virus interaction, viral protein, rna viruses, nucleoprotein, ribonucleoprotein, rna, virion, nucleus, influenza, rna-binding |
| Biological source | INFLUENZA A VIRUS |
| Total number of polymer chains | 9 |
| Total formula weight | 511254.42 |
| Authors | Coloma, R.,Valpuesta, J.M.,Arranz, R.,Carrascosa, J.L.,Ortin, J.,Martin-Benito, J. (deposition date: 2009-04-15, release date: 2009-07-07, Last modification date: 2024-05-08) |
| Primary citation | Coloma, R.,Valpuesta, J.M.,Arranz, R.,Carrascosa, J.L.,Ortin, J.,Martin-Benito, J. The Structure of a Biologically Active Influenza Virus Ribonucleoprotein Complex. Plos Pathog., 5:00491-, 2009 Cited by PubMed Abstract: The influenza viruses contain a segmented, single-stranded RNA genome of negative polarity. Each RNA segment is encapsidated by the nucleoprotein and the polymerase complex into ribonucleoprotein particles (RNPs), which are responsible for virus transcription and replication. Despite their importance, information about the structure of these RNPs is scarce. We have determined the three-dimensional structure of a biologically active recombinant RNP by cryo-electron microscopy. The structure shows a nonameric nucleoprotein ring (at 12 Angstrom resolution) with two monomers connected to the polymerase complex (at 18 Angstrom resolution). Docking the atomic structures of the nucleoprotein and polymerase domains, as well as mutational analyses, has allowed us to define the interactions between the functional elements of the RNP and to propose the location of the viral RNA. Our results provide the first model for a functional negative-stranded RNA virus ribonucleoprotein complex. The structure reported here will serve as a framework to generate a quasi-atomic model of the molecular machine responsible for viral RNA synthesis and to test new models for virus RNA replication and transcription. PubMed: 19557158DOI: 10.1371/JOURNAL.PPAT.1000491 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (12 Å) |
Structure validation
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