+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17030 | |||||||||
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Title | Helical nucleocapsid of the Respiratory Syncytial Virus | |||||||||
Map data | Helical nucleocapsid of the Respiratory Syncytial Virus | |||||||||
Sample |
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Keywords | Helical symmetry / N-RNA / nucleocapsid / RSV / VIRAL PROTEIN | |||||||||
Biological species | Human respiratory syncytial virus A strain Long | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 6.2 Å | |||||||||
Authors | Gonnin L / Desfosses A / Gutsche I | |||||||||
Funding support | France, 1 items
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Citation | Journal: Nat Commun / Year: 2023 Title: Structural landscape of the respiratory syncytial virus nucleocapsids. Authors: Lorène Gonnin / Ambroise Desfosses / Maria Bacia-Verloop / Didier Chevret / Marie Galloux / Jean-François Éléouët / Irina Gutsche / Abstract: Human Respiratory Syncytial Virus (HRSV) is a prevalent cause of severe respiratory infections in children and the elderly. The helical HRSV nucleocapsid is a template for the viral RNA synthesis and ...Human Respiratory Syncytial Virus (HRSV) is a prevalent cause of severe respiratory infections in children and the elderly. The helical HRSV nucleocapsid is a template for the viral RNA synthesis and a scaffold for the virion assembly. This cryo-electron microscopy analysis reveals the non-canonical arrangement of the HRSV nucleocapsid helix, composed of 16 nucleoproteins per asymmetric unit, and the resulting systematic variations in the RNA accessibility. We demonstrate that this unique helical symmetry originates from longitudinal interactions by the C-terminal arm of the HRSV nucleoprotein. We explore the polymorphism of the nucleocapsid-like assemblies, report five structures of the full-length particles and two alternative arrangements formed by a C-terminally truncated nucleoprotein mutant, and demonstrate the functional importance of the identified longitudinal interfaces. We put all these findings in the context of the HRSV RNA synthesis machinery and delineate the structural basis for its further investigation. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17030.map.gz | 44.3 MB | EMDB map data format | |
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Header (meta data) | emd-17030-v30.xml emd-17030.xml | 13.9 KB 13.9 KB | Display Display | EMDB header |
Images | emd_17030.png | 178.4 KB | ||
Others | emd_17030_half_map_1.map.gz emd_17030_half_map_2.map.gz | 301.3 MB 301.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17030 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17030 | HTTPS FTP |
-Validation report
Summary document | emd_17030_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_17030_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_17030_validation.xml.gz | 16.8 KB | Display | |
Data in CIF | emd_17030_validation.cif.gz | 19.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17030 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17030 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_17030.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Helical nucleocapsid of the Respiratory Syncytial Virus | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.145 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Helical nucleocapsid of the Respiratory Syncytial Virus. Half B
File | emd_17030_half_map_1.map | ||||||||||||
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Annotation | Helical nucleocapsid of the Respiratory Syncytial Virus. Half B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Helical nucleocapsid of the Respiratory Syncytial Virus. Half A
File | emd_17030_half_map_2.map | ||||||||||||
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Annotation | Helical nucleocapsid of the Respiratory Syncytial Virus. Half A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Helical nucleocapsid of the human Respiratory Syncytial Virus
Entire | Name: Helical nucleocapsid of the human Respiratory Syncytial Virus |
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Components |
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-Supramolecule #1: Helical nucleocapsid of the human Respiratory Syncytial Virus
Supramolecule | Name: Helical nucleocapsid of the human Respiratory Syncytial Virus type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: Helical nucleocapsid with a non-canonical symmetry formed by the nucleoprotein N of the human RSV upon overexpression in insect cells and encapsidation of cellular RNA |
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Source (natural) | Organism: Human respiratory syncytial virus A strain Long |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 42.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.7000000000000001 µm |
-Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 105.3 Å Applied symmetry - Helical parameters - Δ&Phi: 149.453 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 389540 |
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Startup model | Type of model: NONE |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |