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- PDB-6djy: Fako virus -

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Basic information

Entry
Database: PDB / ID: 6djy
TitleFako virus
Components
  • Clamp protein
  • Major capsid protein
  • Turret protein
KeywordsVIRUS / capsid / virion / Reoviridae / T=2
Function / homologyMajor capsid protein / Turret protein / Clamp protein
Function and homology information
Biological speciesFako virus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsKaelber, J.T. / Jiang, W. / Weaver, S.C. / Auguste, A.J. / Chiu, W.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P41GM103832 United States
Welch FoundationQ1242 United States
CitationJournal: Structure / Year: 2020
Title: Arrangement of the Polymerase Complexes inside a Nine-Segmented dsRNA Virus.
Authors: Jason T Kaelber / Wen Jiang / Scott C Weaver / Albert J Auguste / Wah Chiu /
Abstract: Members of the family Reoviridae package several copies of the viral polymerase complex into their capsid to carry out replication and transcription within viral particles. Classical single-particle ...Members of the family Reoviridae package several copies of the viral polymerase complex into their capsid to carry out replication and transcription within viral particles. Classical single-particle reconstruction encounters difficulties resolving structures such as the intraparticle polymerase complex because refinement can converge to an incorrect map and because the map could depict a nonrepresentative subset of particles or an average of heterogeneous particles. Using the nine-segmented Fako virus, we tested hypotheses for the arrangement and number of polymerase complexes within the virion by measuring how well each hypothesis describes the set of cryoelectron microscopy images of individual viral particles. We find that the polymerase complex in Fako virus binds at ten possible sites despite having only nine genome segments. A single asymmetric configuration describes the arrangement of these complexes in both virions and genome-free capsids. Similarities between the arrangements of Reoviridae with 9, 10, and 11 segments indicate the generalizability of this architecture.
Validation Report
SummaryFull reportAbout validation report
History
DepositionMay 27, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 5, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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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-7944
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  • Superimposition on EM map
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Structure viewerMolecule:
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Assembly

Deposited unit
A: Clamp protein
B: Major capsid protein
C: Major capsid protein
D: Turret protein


Theoretical massNumber of molelcules
Total (without water)434,2024
Polymers434,2024
Non-polymers00
Water0
1
A: Clamp protein
B: Major capsid protein
C: Major capsid protein
D: Turret protein
x 60


Theoretical massNumber of molelcules
Total (without water)26,052,108240
Polymers26,052,108240
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation60
2


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
point symmetry operation1
3
A: Clamp protein
B: Major capsid protein
C: Major capsid protein
D: Turret protein
x 5


  • icosahedral pentamer
  • 2.17 MDa, 20 polymers
Theoretical massNumber of molelcules
Total (without water)2,171,00920
Polymers2,171,00920
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation5
4
A: Clamp protein
B: Major capsid protein
C: Major capsid protein
D: Turret protein
x 6


  • icosahedral 23 hexamer
  • 2.61 MDa, 24 polymers
Theoretical massNumber of molelcules
Total (without water)2,605,21124
Polymers2,605,21124
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation6
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 Clamp protein


Mass: 39589.691 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Fako virus / Strain: CSW77 / References: UniProt: A0A0A0UEE5
#2: Protein Major capsid protein


Mass: 136689.766 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Fako virus / Strain: CSW77 / References: UniProt: A0A0A0U7Z7
#3: Protein Turret protein /


Mass: 121232.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Fako virus / Strain: CSW77 / References: UniProt: A0A0A0U955

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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: Fako virus / Type: VIRUS / Entity ID: 1, 2, 3 / Source: NATURAL
Molecular weightValue: 43 MDa / Experimental value: NO
Source (natural)Organism: Fako virus / Strain: CSW77
Details of virusEmpty: NO / Enveloped: NO / Isolate: STRAIN / Type: VIRION
Natural hostOrganism: Culicinae
Virus shellTriangulation number (T number): 2
Buffer solutionpH: 7.8
Buffer component
IDConc.NameFormulaBuffer-ID
110 mMTris-HClTrisC4H12NO3CL1
21 mMEDTAEthylenediaminetetraacetic acid1
3100 mMsodium chlorideNaClSodium chloride1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: unspecified
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: JEOL 3200FSC
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Cs: 4.7 mm
Specimen holderCryogen: NITROGEN / Model: JEOL 3200FSC CRYOHOLDER
Image recordingElectron dose: 30 e/Å2 / Detector mode: INTEGRATING / Film or detector model: DIRECT ELECTRON DE-20 (5k x 3k) / Num. of real images: 2400
EM imaging opticsEnergyfilter name: In-column Omega Filter

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Processing

SoftwareName: PHENIX / Version: dev_3366: / Classification: refinement
EM software
IDNameCategory
4jsprCTF correction
10jsprinitial Euler assignment
11jsprfinal Euler assignment
13jspr3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 10588
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5294 / Algorithm: FOURIER SPACE / Symmetry type: POINT
Refine LS restraints
Refinement-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00828502
ELECTRON MICROSCOPYf_angle_d0.90238718
ELECTRON MICROSCOPYf_dihedral_angle_d5.19617288
ELECTRON MICROSCOPYf_chiral_restr0.0514507
ELECTRON MICROSCOPYf_plane_restr0.0054910

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