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- EMDB-12792: MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-12792 | |||||||||
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Title | MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173 insertion VLP displaying fullerene C70-like D5 symmetry | |||||||||
![]() | main volume | |||||||||
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Function / homology | ![]() negative regulation of viral translation / T=3 icosahedral viral capsid / regulation of translation / structural molecule activity / RNA binding / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.09 Å | |||||||||
![]() | Biela AP | |||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 328.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.3 KB 11.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.2 KB | Display | ![]() |
Images | ![]() | 3.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | main volume | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.14667 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Escherichia virus MS2
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Escherichia virus MS2
Supramolecule | Name: 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 |
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Host system | Organism: ![]() ![]() |
Molecular weight | Experimental: 3.1 MDa |
Virus shell | Shell ID: 1 / Diameter: 360.0 Å |
-Macromolecule #1: MS2 bacteriophage coat protein dimer
Macromolecule | Name: MS2 bacteriophage coat protein dimer / type: protein_or_peptide / ID: 1 Details: MS2 coat protein dimer with 145-GSGGGGSAHIVMVDAYKPTKGGGSGGSGT-173 insertion Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MASNFTQFVL VDNGGTGDVT VAPSNFASGV AEWISSNSRS QACKVTCSVR QSSAQNRKYA IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP SAIAANSGIY ANFTQFVLVD NGGTGGSGGG SAHIVMVDAY KPTKGGGSGG ...String: MASNFTQFVL VDNGGTGDVT VAPSNFASGV AEWISSNSRS QACKVTCSVR QSSAQNRKYA IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP SAIAANSGIY ANFTQFVLVD NGGTGGSGGG SAHIVMVDAY KPTKGGGSGG SGTGDVTVAP SNFANGVAEW ISSNSRSQAY KVTCSVRQSS AQNRKYTIKV EVPKVATQTV GGVELPVAAW RSYLNMELTI PIFATNSDCE LIVKAMQGLL KDGNPIPSAI AANSGIY |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1 mg/mL |
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Buffer | pH: 7.4 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 101.325 kPa |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 8687 / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |