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- EMDB-12788: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 inser... -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-12788
TitleMS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion VLP displaying fullerene C74-like D3 symmetry
Map datamain volume
Sample
  • Virus: Escherichia virus MS2
    • Protein or peptide: MS2 bacteriophage coat protein dimer
Function / homology
Function and homology information


negative regulation of viral translation / T=3 icosahedral viral capsid / regulation of translation / structural molecule activity / RNA binding / identical protein binding
Similarity search - Function
Levivirus coat protein / Levivirus coat protein / Bacteriophage RNA-type, capsid
Similarity search - Domain/homology
Biological speciesEscherichia phage MS2 (virus) / Escherichia virus MS2
Methodsingle particle reconstruction / cryo EM / Resolution: 3.34 Å
AuthorsBiela AP
Funding support Poland, 2 items
OrganizationGrant numberCountry
Polish National Science Centre2016/20/W/NZ1/00095 Poland
Polish National Science Centre2019/34/A/NZ1/00196 Poland
CitationJournal: Commun Mater / Year: 2022
Title: Programmable polymorphism of a virus-like particle.
Authors: Artur P Biela / Antonina Naskalska / Farzad Fatehi / Reidun Twarock / Jonathan G Heddle /
Abstract: Virus-like particles (VLPs) have significant potential as artificial vaccines and drug delivery systems. The ability to control their size has wide ranging utility but achieving such controlled ...Virus-like particles (VLPs) have significant potential as artificial vaccines and drug delivery systems. The ability to control their size has wide ranging utility but achieving such controlled polymorphism using a single protein subunit is challenging as it requires altering VLP geometry. Here we achieve size control of MS2 bacteriophage VLPs via insertion of amino acid sequences in an external loop to shift morphology to significantly larger forms. The resulting VLP size and geometry is controlled by altering the length and type of the insert. Cryo electron microscopy structures of the new VLPs, in combination with a kinetic model of their assembly, show that the abundance of wild type ( = 3), = 4, D3 and D5 symmetrical VLPs can be biased in this way. We propose a mechanism whereby the insert leads to a change in the dynamic behavior of the capsid protein dimer, affecting the interconversion between the symmetric and asymmetric conformers and thus determining VLP size and morphology.
History
DepositionApr 20, 2021-
Header (metadata) releaseFeb 16, 2022-
Map releaseFeb 16, 2022-
UpdateFeb 16, 2022-
Current statusFeb 16, 2022Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.93
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.93
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_12788.png

Downloads & links

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Map

FileDownload / File: emd_12788.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmain volume
Voxel sizeX=Y=Z: 1.14667 Å
Density
Contour LevelBy AUTHOR: 0.934 / Movie #1: 0.93
Minimum - Maximum-2.1993985 - 4.9867134
Average (Standard dev.)0.01117483 (±0.27262595)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 516.0001 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.14666666666671.14666666666671.1466666666667
M x/y/z450450450
origin x/y/z0.0000.0000.000
length x/y/z516.000516.000516.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS450450450
D min/max/mean-2.1994.9870.011

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Supplemental data

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Sample components

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Entire : Escherichia virus MS2

EntireName: Escherichia virus MS2
Components
  • Virus: Escherichia virus MS2
    • Protein or peptide: MS2 bacteriophage coat protein dimer

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Supramolecule #1: Escherichia virus MS2

SupramoleculeName: Escherichia virus MS2 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 329852 / Sci species name: Escherichia virus MS2 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes
Host systemOrganism: Escherichia coli (E. coli)
Molecular weightExperimental: 3.3 MDa
Virus shellShell ID: 1 / Diameter: 340.0 Å

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Macromolecule #1: MS2 bacteriophage coat protein dimer

MacromoleculeName: MS2 bacteriophage coat protein dimer / type: protein_or_peptide / ID: 1
Details: MS2 coat protein dimer with 145-GGGSYATMPIAKHVKDVGGGSGT-167 insertion
Enantiomer: LEVO
Source (natural)Organism: Escherichia phage MS2 (virus)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MASNFTPFVL VDNGGTGDVT VAPSNFANGV AEWISSNSRS QAYKVTCSVR QSSAQNRKYT IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP SAIAANSGIY ANFTQFVLVD NGGTGGGSYA TMPIAKHVKD VGGGSGTGDV ...String:
MASNFTPFVL VDNGGTGDVT VAPSNFANGV AEWISSNSRS QAYKVTCSVR QSSAQNRKYT IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP SAIAANSGIY ANFTQFVLVD NGGTGGGSYA TMPIAKHVKD VGGGSGTGDV TVAPSNFANG VAEWISSNSR SQAYKVTCSV RQSSAQNRKY TIKVEVPKVA TQTVGGVELP VAAWRSYLNM ELTIPIFATN SDCELIVKAM QGLLKDGNPI PSAIAANSGI Y

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 7.4
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 101.325 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 4546 / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 539
CTF correctionSoftware - Name: Warp (ver. 1.0.9)
Final reconstructionApplied symmetry - Point group: D3 (2x3 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 3.34 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2.15.0) / Number images used: 12714
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: cryoSPARC (ver. 2.15.0)
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: cryoSPARC (ver. 2.15.0)
Final 3D classificationNumber classes: 3
FSC plot (resolution estimation)

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