|Entry||Database: EMDB / ID: EMD-21261|
|Title||Asymmetry reconstruction of Brome mosaic virus (RNA 3 and 4)|
|Biological species||Brome mosaic virus|
|Method||single particle reconstruction / cryo EM / Resolution: 3.9 Å|
|Authors||Beren C / Cui YX / Chakravarty A / Yang X / Rao ALN / Knobler CM / Zhou ZH / Gelbart WM|
|Funding support|| United States, 2 items |
|Citation||Journal: Proc Natl Acad Sci U S A / Year: 2020|
Title: Genome organization and interaction with capsid protein in a multipartite RNA virus.
Authors: Christian Beren / Yanxiang Cui / Antara Chakravarty / Xue Yang / A L N Rao / Charles M Knobler / Z Hong Zhou / William M Gelbart /
Abstract: We report the asymmetric reconstruction of the single-stranded RNA (ssRNA) content in one of the three otherwise identical virions of a multipartite RNA virus, brome mosaic virus (BMV). We exploit a ...We report the asymmetric reconstruction of the single-stranded RNA (ssRNA) content in one of the three otherwise identical virions of a multipartite RNA virus, brome mosaic virus (BMV). We exploit a sample consisting exclusively of particles with the same RNA content-specifically, RNAs 3 and 4-assembled in planta by agrobacterium-mediated transient expression. We find that the interior of the particle is nearly empty, with most of the RNA genome situated at the capsid shell. However, this density is disordered in the sense that the RNA is not associated with any particular structure but rather, with an ensemble of secondary/tertiary structures that interact with the capsid protein. Our results illustrate a fundamental difference between the ssRNA organization in the multipartite BMV viral capsid and the monopartite bacteriophages MS2 and Qβ for which a dominant RNA conformation is found inside the assembled viral capsids, with RNA density conserved even at the center of the particle. This can be understood in the context of the differing demands on their respective lifecycles: BMV must package separately each of several different RNA molecules and has been shown to replicate and package them in isolated, membrane-bound, cytoplasmic complexes, whereas the bacteriophages exploit sequence-specific "packaging signals" throughout the viral RNA to package their monopartite genomes.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_21261.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.07 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire : Brome mosaic virus
|Entire||Name: Brome mosaic virus|
-Supramolecule #1: Brome mosaic virus
|Supramolecule||Name: Brome mosaic virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 / NCBI-ID: 12302 / Sci species name: Brome mosaic virus / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No|
|Processing||single particle reconstruction|
|Vitrification||Cryogen name: ETHANE-PROPANE|
|Microscope||FEI TITAN KRIOS|
|Electron beam||Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy|
|Sample stage||Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN|
|Image recording||Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 1-30 / Average electron dose: 48.0 e/Å2|
Model: Titan Krios / Image courtesy: FEI Company
|Startup model||Type of model: OTHER / Details: a Gaussian ball|
|Initial angle assignment||Type: MAXIMUM LIKELIHOOD|
|Final angle assignment||Type: MAXIMUM LIKELIHOOD|
|Final reconstruction||Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 70470|
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