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Yorodumi- EMDB-17046: Virus-like Particle based on PVY coat protein with stacked-ring a... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17046 | |||||||||
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Title | Virus-like Particle based on PVY coat protein with stacked-ring architecture | |||||||||
Map data | VLPr sharp symmetric cryoEM map (C8) | |||||||||
Sample |
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Keywords | stacked-ring / VLP / Potyvirus / PVY / VIRUS LIKE PARTICLE | |||||||||
Function / homology | Potyvirus coat protein / Potyvirus coat protein / viral capsid / Genome polyprotein Function and homology information | |||||||||
Biological species | Potato virus Y strain NTN | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.34 Å | |||||||||
Authors | Kavcic L / Kezar A / Podobnik M | |||||||||
Funding support | Slovenia, 2 items
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Citation | Journal: Commun Chem / Year: 2024 Title: From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y. Authors: Luka Kavčič / Andreja Kežar / Neža Koritnik / Magda Tušek Žnidarič / Tajda Klobučar / Žiga Vičič / Franci Merzel / Ellie Holden / Justin L P Benesch / Marjetka Podobnik / Abstract: The structural diversity and tunability of the capsid proteins (CPs) of various icosahedral and rod-shaped viruses have been well studied and exploited in the development of smart hybrid ...The structural diversity and tunability of the capsid proteins (CPs) of various icosahedral and rod-shaped viruses have been well studied and exploited in the development of smart hybrid nanoparticles. However, the potential of CPs of the wide-spread flexuous filamentous plant viruses remains to be explored. Here, we show that we can control the shape, size, RNA encapsidation ability, symmetry, stability and surface functionalization of nanoparticles through structure-based design of CP from potato virus Y (PVY). We provide high-resolution insight into CP-based self-assemblies, ranging from large polymorphic or monomorphic filaments to smaller annular, cubic or spherical particles. Furthermore, we show that we can prevent CP self-assembly in bacteria by fusion with a cleavable protein, enabling controlled nanoparticle formation in vitro. Understanding the remarkable structural diversity of PVY CP not only provides possibilities for the production of biodegradable nanoparticles, but may also advance future studies of CP's polymorphism in a biological context. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17046.map.gz | 22.1 MB | EMDB map data format | |
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Header (meta data) | emd-17046-v30.xml emd-17046.xml | 19.1 KB 19.1 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17046_fsc.xml | 9.9 KB | Display | FSC data file |
Images | emd_17046.png | 69.4 KB | ||
Masks | emd_17046_msk_1.map | 103 MB | Mask map | |
Filedesc metadata | emd-17046.cif.gz | 6.3 KB | ||
Others | emd_17046_additional_1.map.gz emd_17046_half_map_1.map.gz emd_17046_half_map_2.map.gz | 50.8 MB 95.3 MB 95.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17046 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17046 | HTTPS FTP |
-Validation report
Summary document | emd_17046_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_17046_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_17046_validation.xml.gz | 18.1 KB | Display | |
Data in CIF | emd_17046_validation.cif.gz | 23.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17046 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17046 | HTTPS FTP |
-Related structure data
Related structure data | 8opaMC 8opbC 8opcC 8opdC 8opeC 8opfC 8opgC 8ophC 8opjC 8opkC 8oplC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_17046.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | VLPr sharp symmetric cryoEM map (C8) | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.95 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_17046_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: VLPr raw cryoEM map (C8)
File | emd_17046_additional_1.map | ||||||||||||
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Annotation | VLPr raw cryoEM map (C8) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: VLPr half B cryoEM map
File | emd_17046_half_map_1.map | ||||||||||||
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Annotation | VLPr half B cryoEM map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: VLPr half A cryoEM map
File | emd_17046_half_map_2.map | ||||||||||||
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Annotation | VLPr half A cryoEM map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Virus-like particle from PVY coat protein
Entire | Name: Virus-like particle from PVY coat protein |
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Components |
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-Supramolecule #1: Virus-like particle from PVY coat protein
Supramolecule | Name: Virus-like particle from PVY coat protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: The sample contains 3 forms of filaments. |
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Source (natural) | Organism: Potato virus Y strain NTN |
-Macromolecule #1: Genome polyprotein (Fragment)
Macromolecule | Name: Genome polyprotein (Fragment) / type: protein_or_peptide / ID: 1 Details: Due to flexibility, structural model could only be built from H42 to A222. Number of copies: 24 / Enantiomer: LEVO |
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Source (natural) | Organism: Potato virus Y strain NTN / Strain: NTN |
Molecular weight | Theoretical: 29.935797 KDa |
Recombinant expression | Organism: Escherichia coli BL21(DE3) (bacteria) |
Sequence | String: GNDTIDAGGS TKKDAKQEQG SIQPNLNKEK EKDVNVGTSG THTVPRIKAI TSKMRMPKSK GATVLNLEHL LEYAPQQIDI SNTRATQSQ FDTWYEAVQL AYDIGETEMP TVMNGLMVWC IENGTSPNIN GVWVMMDGDE QVEYPLKPIV ENAKPTLRQI M AHFSDVAE ...String: GNDTIDAGGS TKKDAKQEQG SIQPNLNKEK EKDVNVGTSG THTVPRIKAI TSKMRMPKSK GATVLNLEHL LEYAPQQIDI SNTRATQSQ FDTWYEAVQL AYDIGETEMP TVMNGLMVWC IENGTSPNIN GVWVMMDGDE QVEYPLKPIV ENAKPTLRQI M AHFSDVAE AYIEMRNKKE PYMPRYGLVR NLRDGSLARY AFDFYEVTSR TPVRAREAHI QMKAAALKSA QSRLFGLDGG IS TQEENTE RHTTEDVSPS MHTLLGVKNM UniProtKB: Genome polyprotein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | filament |
-Sample preparation
Concentration | 1 mg/mL |
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Buffer | pH: 7.4 Details: 1.8 mM KH2PO4, 10.1 mM Na2HPO4, 140 mM NaCl, 2.7 mM KCl, pH 7.4 |
Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number real images: 502 / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.1 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 150000 |
Sample stage | Cooling holder cryogen: NITROGEN |