4BBL
Cryo-electron microscopy reconstruction of the helical part of influenza A virus ribonucleoprotein isolated from virions.
Summary for 4BBL
| Entry DOI | 10.2210/pdb4bbl/pdb |
| EMDB information | 2205 |
| Descriptor | NUCLEOPROTEIN, RNA (2 entities in total) |
| Functional Keywords | nuclear protein, nucleocapsid |
| Biological source | INFLUENZA A VIRUS More |
| Cellular location | Virion : P15682 |
| Total number of polymer chains | 26 |
| Total formula weight | 1551852.88 |
| Authors | Arranz, R.,Coloma, R.,Chichon, F.J.,Conesa, J.J.,Carrascosa, J.L.,Valpuesta, J.M.,Ortin, J.,Martin-Benito, J. (deposition date: 2012-09-26, release date: 2012-12-05, Last modification date: 2024-05-08) |
| Primary citation | Arranz, R.,Coloma, R.,Chichon, F.J.,Conesa, J.J.,Carrascosa, J.L.,Valpuesta, J.M.,Ortin, J.,Martin-Benito, J. The Structure of Native Influenza Virion Ribonucleoproteins Science, 338:1634-, 2012 Cited by PubMed Abstract: The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented negative-stranded RNAs are associated with the polymerase complex and nucleoprotein (NP), forming ribonucleoproteins (RNPs), which are responsible for virus transcription and replication. We describe the structure of native RNPs derived from virions. They show a double-helical conformation in which two NP strands of opposite polarity are associated with each other along the helix. Both strands are connected by a short loop at one end of the particle and interact with the polymerase complex at the other end. This structure will be relevant for unraveling the mechanisms of nuclear import of parental virus RNPs, their transcription and replication, and the encapsidation of progeny RNPs into virions. PubMed: 23180776DOI: 10.1126/SCIENCE.1228172 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (18 Å) |
Structure validation
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