Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into influenza A virus ribonucleoproteins reveal a processive helical track as transcription mechanism.
Journal, issue, pages	Nat Microbiol, Vol. 5, Issue 5, Page 727-734, Year 2020
Publish date	Mar 9, 2020
Authors	Rocío Coloma / Rocío Arranz / José M de la Rosa-Trevín / Carlos O S Sorzano / Sandie Munier / Diego Carlero / Nadia Naffakh / Juan Ortín / Jaime Martín-Benito /
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 ...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.
External links	Nat Microbiol / PubMed:32152587
Methods	EM (helical sym.)
Resolution	10.0 - 24.0 Å
Structure data	0175 6h9g EMDB-0175: Helical part of the influenza A virus ribonucleoprotein. Conformation 1. PDB-6h9g: Influenza A nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 1. Method: EM (helical sym.) / Resolution: 11.0 Å 4412 6i54 EMDB-4412: Helical part of the influenza A virus ribonucleoprotein. Conformation 2. PDB-6i54: Influenza A nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 2. Method: EM (helical sym.) / Resolution: 10.0 Å 4423 6i7b EMDB-4423: Helical part of the influenza A virus ribonucleoprotein. Conformation 3. PDB-6i7b: Influenza A nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 3. Method: EM (helical sym.) / Resolution: 10.0 Å 4426 6i7m EMDB-4426: Helical part of the influenza A virus ribonucleoprotein. Conformation 4. PDB-6i7m: Influenza A nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 4. Method: EM (helical sym.) / Resolution: 10.0 Å 4430 6i85 EMDB-4430: Helical part of the influenza A virus ribonucleoprotein. Conformation 5. PDB-6i85: Influenza A nucleoprotein docked into the 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 5. Method: EM (helical sym.) / Resolution: 24.0 Å
Source	influenza a virus Influenza A virus (strain A/WS/1933 H1N1) influenza a virus (a/wilson-smith/1933(h1n1)) influenza a virus (strain a/wilson-smith/1933 h1n1)
Keywords	VIRAL PROTEIN / Influenza A virus Ribonucleoprotein RNA binding protein / Influenza A virus / Ribonucleoprotein / RNA binding protein / RNA binding protein.