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Yorodumi- EMDB-61933: Hexameric flat ring-like complex of the Borna disease virus 1 nuc... -
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Basic information
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| Title | Hexameric flat ring-like complex of the Borna disease virus 1 nucleoprotein (mutant Lys164Ala) | |||||||||
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Keywords | nucleoprotein / complex / VIRAL PROTEIN | |||||||||
| Biological species | Borna disease virus 1 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 6.26 Å | |||||||||
Authors | Goto SH / Sugita Y / Hirai Y / Horie M | |||||||||
| Funding support | Japan, 2 items
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Citation | Journal: Sci Adv / Year: 2026Title: Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes. Authors: Yukihiko Sugita / Yuya Hirai / Shinya H Goto / Takuro Fujiwara / Keizo Tomonaga / Takeshi Noda / Masayuki Horie / ![]() Abstract: Structures of nucleoprotein (N)-RNA complexes of the , a virus family in the order , have not been reported. Here, using cryo-electron microscopy (cryo-EM), we report high-resolution structures of ...Structures of nucleoprotein (N)-RNA complexes of the , a virus family in the order , have not been reported. Here, using cryo-electron microscopy (cryo-EM), we report high-resolution structures of Borna disease virus 1 (BoDV-1) N-RNA complex assemblies, including a dominant hexameric ring-like complex and less populated heptameric and octameric forms, the first RNA-bound N structures reported from this family. These structures reveal key features of N-RNA engagement and a BoDV-1-specific stoichiometry of eight nucleotides per N, providing a framework for comparison with related negative-strand RNA viruses. In addition to these RNA-bound complexes, we identified multiple RNA-free oligomers, indicating substantial conformational flexibility of N. Mutational analyses identified residues essential for nucleocapsid formation and RNA synthesis. Cryo-EM of mutant complexes captured RNA-free assemblies, suggesting that initial N oligomerization precedes RNA binding. These findings clarify the structural organization of the N-RNA complex and suggest how oligomeric plasticity contributes to nucleocapsid assembly. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_61933.map.gz | 7.1 MB | EMDB map data format | |
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| Header (meta data) | emd-61933-v30.xml emd-61933.xml | 17.1 KB 17.1 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_61933_fsc.xml | 6.9 KB | Display | FSC data file |
| Images | emd_61933.png | 47.4 KB | ||
| Masks | emd_61933_msk_1.map | 7.6 MB | Mask map | |
| Filedesc metadata | emd-61933.cif.gz | 5.4 KB | ||
| Others | emd_61933_half_map_1.map.gz emd_61933_half_map_2.map.gz | 7.1 MB 7.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-61933 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-61933 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_61933.map.gz / Format: CCP4 / Size: 7.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.448 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_61933_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_61933_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_61933_half_map_2.map | ||||||||||||
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Sample components
-Entire : Purified Borna disease virus 1 nucleoprotein (mutant Lys164Ala)
| Entire | Name: Purified Borna disease virus 1 nucleoprotein (mutant Lys164Ala) |
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| Components |
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-Supramolecule #1: Purified Borna disease virus 1 nucleoprotein (mutant Lys164Ala)
| Supramolecule | Name: Purified Borna disease virus 1 nucleoprotein (mutant Lys164Ala) type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Borna disease virus 1 / Strain: He/80 |
-Macromolecule #1: Nucleoprotein of the Borna disease virus 1 (mutant Lys164Ala)
| Macromolecule | Name: Nucleoprotein of the Borna disease virus 1 (mutant Lys164Ala) type: protein_or_peptide / ID: 1 Details: Full-length nucleoprotein (mutant Lys164Ala) of the Borna disease virus 1 strain He/80 with N-terminal hexahistidine tag Enantiomer: LEVO |
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| Source (natural) | Organism: Borna disease virus 1 / Strain: He/80 |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGSSHHHHHH SSGLVPRGSH MLE MPPKRR LVDDADAMED QDLYEPPASL PKLPGKFLQY TVGGSDPHPG IGHEKDIRQN AVAL LDQSR RDMFHTVTPS LVFLCLLIPG LHAAFVHGGV PRESYLSTPV TRGEQTVVKT AKFYG EKTT QRDLTELEIS SIFSHCCSLL ...String: MGSSHHHHHH SSGLVPRGSH MLE MPPKRR LVDDADAMED QDLYEPPASL PKLPGKFLQY TVGGSDPHPG IGHEKDIRQN AVAL LDQSR RDMFHTVTPS LVFLCLLIPG LHAAFVHGGV PRESYLSTPV TRGEQTVVKT AKFYG EKTT QRDLTELEIS SIFSHCCSLL IGVVIGSSSK IKAGAEQIKA RFKTMMAALN RPSHGE TAT LLQMFNPHEA IDWINGQPWV GSFVLSLLTT DFESPGKEFM DQIKLVASYA QMTTYTT IK EYLAECMDAT LTIPVVAYEI RDFLEVSAKL KEEHADLFPF LGAIRHPDAI KLAPRSFP N LASAAFYWSK KENPTMAGYR ASTIQPGASV KETQLARYRR REISRGEDGA ELSGEISAI MRMIGVTGLN |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 43.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm |
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Image processing
-Atomic model buiding 1
| Initial model | PDB ID: Chain - Source name: PDB / Chain - Initial model type: experimental model |
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| Refinement | Space: RECIPROCAL / Protocol: AB INITIO MODEL |
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About Yorodumi



Keywords
Borna disease virus 1
Authors
Japan, 2 items
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FIELD EMISSION GUN

