6I85

Influenza A nucleoprotein docked into the 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 5.

Summary for 6I85

• Entry DOI: 10.2210/pdb6i85/pdb
• EMDB information: 0175 4412 4423 4426 4430
• Descriptor: Influenza A nucleoprotein, Nucleoprotein (2 entities in total)
• Functional Keywords: influenza a virus, ribonucleoprotein, rna binding protein., viral protein
• Biological source: Influenza A virus (strain A/Wilson-Smith/1933 H1N1); More
• Total number of polymer chains: 4
• Total formula weight: 96125.82

Authors

Coloma, R.,Arranz, R.,de la Rosa-Trevin, J.M.,Sorzano, C.O.S.,Carlero, D.,Ortin, J.,Martin-Benito, J. (deposition date: 2018-11-19, release date: 2020-01-29, Last modification date: 2024-05-15)

Primary citation

Coloma, R.,Arranz, R.,de la Rosa-Trevin, J.M.,Sorzano, C.O.S.,Munier, S.,Carlero, D.,Naffakh, N.,Ortin, J.,Martin-Benito, J.
Structural insights into influenza A virus ribonucleoproteins reveal a processive helical track as transcription mechanism.
Nat Microbiol, 5:727-734, 2020

PubMed Abstract: The influenza virus genome consists of eight viral ribonucleoproteins (vRNPs), each consisting of a copy of the polymerase, one of the genomic RNA segments and multiple copies of the nucleoprotein arranged in a double helical conformation. vRNPs are macromolecular machines responsible for messenger RNA synthesis and genome replication, that is, the formation of progeny vRNPs. Here, we describe the structural basis of the transcription process. The mechanism, which we call the 'processive helical track', is based on the extreme flexibility of the helical part of the vRNP that permits a sliding movement between both antiparallel nucleoprotein-RNA strands, thereby allowing the polymerase to move over the genome while bound to both RNA ends. Accordingly, we demonstrate that blocking this movement leads to inhibition of vRNP transcriptional activity. This mechanism also reveals a critical role of the nucleoprotein in maintaining the double helical structure throughout the copying process to make the RNA template accessible to the polymerase.

PubMed: 32152587
DOI: 10.1038/s41564-020-0675-3

Experimental method

ELECTRON MICROSCOPY (24 Å)