+Open data
-Basic information
Entry | Database: PDB / ID: 7ewq | ||||||
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Title | Structure of Mumps virus nucleocapsid ring | ||||||
Components |
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Keywords | NUCLEAR PROTEIN / nucleocapcid / Mumps virus | ||||||
Function / homology | Function and homology information helical viral capsid / viral nucleocapsid / host cell cytoplasm / ribonucleoprotein complex / structural molecule activity / RNA binding Similarity search - Function | ||||||
Biological species | Mumps virus Mumps orthorubulavirus | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Su, X. / Shen, Q. / Shan, H. | ||||||
Funding support | China, 1items
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Citation | Journal: Commun Biol / Year: 2021 Title: Structural plasticity of mumps virus nucleocapsids with cryo-EM structures. Authors: Hong Shan / Xin Su / Tianhao Li / Yuqi Qin / Na Zhang / Liuyan Yang / Linsha Ma / Yun Bai / Lei Qi / Yunhui Liu / Qing-Tao Shen / Abstract: Mumps virus (MuV) is a highly contagious human pathogen and frequently causes worldwide outbreaks despite available vaccines. Similar to other mononegaviruses such as Ebola and rabies, MuV uses a ...Mumps virus (MuV) is a highly contagious human pathogen and frequently causes worldwide outbreaks despite available vaccines. Similar to other mononegaviruses such as Ebola and rabies, MuV uses a single-stranded negative-sense RNA as its genome, which is enwrapped by viral nucleoproteins into the helical nucleocapsid. The nucleocapsid acts as a scaffold for genome condensation and as a template for RNA replication and transcription. Conformational changes in the MuV nucleocapsid are required to switch between different activities, but the underlying mechanism remains elusive due to the absence of high-resolution structures. Here, we report two MuV nucleoprotein-RNA rings with 13 and 14 protomers, one stacked-ring filament and two nucleocapsids with distinct helical pitches, in dense and hyperdense states, at near-atomic resolutions using cryo-electron microscopy. Structural analysis of these in vitro assemblies indicates that the C-terminal tail of MuV nucleoprotein likely regulates the assembly of helical nucleocapsids, and the C-terminal arm may be relevant for the transition between the dense and hyperdense states of helical nucleocapsids. Our results provide the molecular mechanism for structural plasticity among different MuV nucleocapsids and create a possible link between structural plasticity and genome condensation. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7ewq.cif.gz | 84.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7ewq.ent.gz | 60.6 KB | Display | PDB format |
PDBx/mmJSON format | 7ewq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7ewq_validation.pdf.gz | 900.2 KB | Display | wwPDB validaton report |
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Full document | 7ewq_full_validation.pdf.gz | 906.4 KB | Display | |
Data in XML | 7ewq_validation.xml.gz | 30.7 KB | Display | |
Data in CIF | 7ewq_validation.cif.gz | 44 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/7ewq ftp://data.pdbj.org/pub/pdb/validation_reports/ew/7ewq | HTTPS FTP |
-Related structure data
Related structure data | 31361MC 7exaC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Symmetry | Point symmetry: (Schoenflies symbol: C13 (13 fold cyclic)) |
-Components
#1: Protein | Mass: 61470.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mumps virus (strain Jeryl-Lynn) / Strain: Jeryl-Lynn / Gene: N, NP / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q77IS8 |
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#2: RNA chain | Mass: 1792.037 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mumps orthorubulavirus / Production host: Escherichia coli BL21(DE3) (bacteria) |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Mumps virus nocleocapcid / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||
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Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: NO | |||||||||||||||
Source (natural) | Organism: Mumps rubulavirus | |||||||||||||||
Source (recombinant) | Organism: Escherichia coli BL21(DE3) (bacteria) / Plasmid: pET28b | |||||||||||||||
Buffer solution | pH: 7.4 | |||||||||||||||
Buffer component |
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Specimen | Conc.: 0.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
3D reconstruction | Resolution: 3.5 Å / Num. of particles: 390418 / Symmetry type: POINT | |||||||||
Refinement | Highest resolution: 3.5 Å |