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- PDB-6voc: icosahedral symmetry reconstruction of brome mosaic virus (RNA 3+4) -

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Basic information

Entry
Database: PDB / ID: 6voc
Titleicosahedral symmetry reconstruction of brome mosaic virus (RNA 3+4)
ComponentsCapsid protein
KeywordsVIRUS / Brome mosaic virus (RNA 3 and 4)
Function / homology
Function and homology information


T=3 icosahedral viral capsid / host cell endoplasmic reticulum / viral nucleocapsid / ribonucleoprotein complex / structural molecule activity / RNA binding
Similarity search - Function
Satellite virus coat domain / Bromovirus coat protein / Bromovirus coat protein / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesBrome mosaic virus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsBeren, C. / Cui, Y.X. / Chakravarty, A. / Yang, X. / Rao, A.L.N. / Knobler, C.M. / Zhou, Z.H. / Gelbart, W.M.
Funding support United States, 2items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States) United States
National Institutes of Health/National Institute on Alcohol Abuse and Alcoholism (NIH/NIAAA) United States
CitationJournal: 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.
History
DepositionJan 30, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 20, 2020Provider: repository / Type: Initial release
Revision 1.1May 27, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Mar 6, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type

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Structure visualization

Movie
  • Biological unit as complete icosahedral assembly
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  • Biological unit as icosahedral pentamer
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  • Biological unit as icosahedral 23 hexamer
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  • Deposited structure unit
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  • Simplified surface model + fitted atomic model
  • EMDB-21260
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  • Superimposition on EM map
  • EMDB-21260
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Structure viewerMolecule:
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Assembly

Deposited unit
B: Capsid protein
C: Capsid protein
A: Capsid protein


Theoretical massNumber of molelcules
Total (without water)61,2353
Polymers61,2353
Non-polymers00
Water00
1
B: Capsid protein
C: Capsid protein
A: Capsid protein
x 60


Theoretical massNumber of molelcules
Total (without water)3,674,075180
Polymers3,674,075180
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
2


  • Idetical with deposited unit
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
B: Capsid protein
C: Capsid protein
A: Capsid protein
x 5


  • icosahedral pentamer
  • 306 kDa, 15 polymers
Theoretical massNumber of molelcules
Total (without water)306,17315
Polymers306,17315
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
B: Capsid protein
C: Capsid protein
A: Capsid protein
x 6


  • icosahedral 23 hexamer
  • 367 kDa, 18 polymers
Theoretical massNumber of molelcules
Total (without water)367,40718
Polymers367,40718
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
SymmetryPoint symmetry: (Schoenflies symbol: I (icosahedral))

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Components

#1: Protein Capsid protein / CP / Coat protein


Mass: 20411.525 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Brome mosaic virus / Gene: ORF3b / Production host: Nicotiana benthamiana (plant) / References: UniProt: P03602

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Brome mosaic virus / Type: VIRUS / Entity ID: all / Source: NATURAL
Source (natural)Organism: Brome mosaic virus
Details of virusEmpty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION
Buffer solutionpH: 7.2
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Calibrated defocus min: 8000 nm / Calibrated defocus max: 30000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: NONE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 48 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)
EM imaging opticsEnergyfilter name: GIF Quantum LS / Chromatic aberration corrector: none / Energyfilter slit width: 20 eV / Spherical aberration corrector: none
Image scansMovie frames/image: 30 / Used frames/image: 1-30

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Processing

SoftwareName: PHENIX / Version: dev_2666: / Classification: refinement
EM softwareName: SerialEM / Version: 3.6 / Category: image acquisition / Details: SerialEM was used to automatically obtain images
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 70470 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0063636
ELECTRON MICROSCOPYf_angle_d0.8534948
ELECTRON MICROSCOPYf_dihedral_angle_d4.0062197
ELECTRON MICROSCOPYf_chiral_restr0.059596
ELECTRON MICROSCOPYf_plane_restr0.006624

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