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Yorodumi- EMDB-1206: Structure of the bacteriophage phi6 nucleocapsid suggests a mecha... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1206 | |||||||||
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Title | Structure of the bacteriophage phi6 nucleocapsid suggests a mechanism for sequential RNA packaging. | |||||||||
Map data | Reconstruction of phi6 nucleocapsid to 7.5-A resolution | |||||||||
Sample |
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Function / homology | : / Major inner capsid protein P1 / T=2 icosahedral viral capsid / viral inner capsid / viral nucleocapsid / RNA binding / identical protein binding / Major inner protein P1 Function and homology information | |||||||||
Biological species | Pseudomonas phage phi6 (bacteriophage) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.5 Å | |||||||||
Authors | Huiskonen JT / de Haas F / Bubeck D / Bamford DH / Fuller SD / Butcher SJ | |||||||||
Citation | Journal: Structure / Year: 2006 Title: Structure of the bacteriophage phi6 nucleocapsid suggests a mechanism for sequential RNA packaging. Authors: Juha T Huiskonen / Felix de Haas / Doryen Bubeck / Dennis H Bamford / Stephen D Fuller / Sarah J Butcher / Abstract: Bacteriophage phi6 is an enveloped dsRNA virus with a segmented genome. Phi6 specifically packages one copy of each of its three genome segments into a preassembled polymerase complex. This leads to ...Bacteriophage phi6 is an enveloped dsRNA virus with a segmented genome. Phi6 specifically packages one copy of each of its three genome segments into a preassembled polymerase complex. This leads to expansion of the polymerase complex, minus and plus strand RNA synthesis, and assembly of the nucleocapsid. The phi6 in vitro assembly and packaging system is a valuable model for dsRNA virus replication. The structure of the nucleocapsid at 7.5 A resolution presented here reveals the secondary structure of the two major capsid proteins. Asymmetric P1 dimers organize as an inner T = 1 shell, and P8 trimers organize as an outer T = 13 laevo shell. The organization of the P1 molecules in the unexpanded and expanded polymerase complex suggests that the expansion is accomplished by rigid body movements of the P1 monomers. This leads to exposure of new potential RNA binding surfaces to control the sequential packaging of the genome segments. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1206.map.gz | 123.6 MB | EMDB map data format | |
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Header (meta data) | emd-1206-v30.xml emd-1206.xml | 22 KB 22 KB | Display Display | EMDB header |
Images | 1206.gif | 35.8 KB | ||
Masks | emd_1206_msk_1.map emd_1206_msk_2.map emd_1206_msk_3.map emd_1206_msk_4.map emd_1206_msk_5.map emd_1206_msk_6.map emd_1206_msk_7.map | 142.3 MB 60.3 MB 142.3 MB 142.3 MB 142.3 MB 142.3 MB 17.7 MB | Mask map | |
Others | MASKnames emd_1206_fsc.jpg | 304 B 131.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1206 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1206 | HTTPS FTP |
-Validation report
Summary document | emd_1206_validation.pdf.gz | 306.4 KB | Display | EMDB validaton report |
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Full document | emd_1206_full_validation.pdf.gz | 305.5 KB | Display | |
Data in XML | emd_1206_validation.xml.gz | 7.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1206 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1206 | HTTPS FTP |
-Related structure data
Related structure data | 4btqM 1207C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_1206.map.gz / Format: CCP4 / Size: 278 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Reconstruction of phi6 nucleocapsid to 7.5-A resolution | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Segmentation: Alpha subunit
Annotation | Alpha subunit | ||||||||||||
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File | emd_1206_msk_1.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Segmentation: Beta subunit
Annotation | Beta subunit | ||||||||||||
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File | emd_1206_msk_2.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Segmentation: Q subunit
Annotation | Q subunit | ||||||||||||
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File | emd_1206_msk_3.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Segmentation: R subunit
Annotation | R subunit | ||||||||||||
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File | emd_1206_msk_4.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Segmentation: S subunit
Annotation | S subunit | ||||||||||||
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File | emd_1206_msk_5.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Segmentation: T subunit
Annotation | T subunit | ||||||||||||
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File | emd_1206_msk_6.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Segmentation: tc B
Annotation | tc_B | ||||||||||||
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File | emd_1206_msk_7.map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Others
Details | [MASKnames] emd_1206_msk_1.map > phi6nc_210_tc_B_mask.map emd_1206_msk_2.map > phi6nc_421_A_mask.map emd_1206_msk_3.map > phi6nc_421_B_mask.map emd_1206_msk_4.map > phi6nc_421_Q_mask.map emd_1206_msk_5.map > phi6nc_421_R_mask.map emd_1206_msk_6.map > phi6nc_421_S_mask.map emd_1206_msk_7.map > phi6nc_421_T_mask.ma |
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Image |
-Sample components
-Entire : Bacteriophage phi6 nucleocapsid
Entire | Name: Bacteriophage phi6 nucleocapsid |
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Components |
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-Supramolecule #1000: Bacteriophage phi6 nucleocapsid
Supramolecule | Name: Bacteriophage phi6 nucleocapsid / type: sample / ID: 1000 / Number unique components: 1 |
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Molecular weight | Theoretical: 22 MDa |
-Supramolecule #1: Pseudomonas phage phi6
Supramolecule | Name: Pseudomonas phage phi6 / type: virus / ID: 1 / Name.synonym: Bacteriophage phi6 / NCBI-ID: 10879 / Sci species name: Pseudomonas phage phi6 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: Yes / Virus empty: No / Syn species name: Bacteriophage phi6 |
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Host (natural) | Organism: Pseudomonas syringae pv phaesolicola HB10Y / synonym: BACTERIA(EUBACTERIA) |
Virus shell | Shell ID: 1 / Name: PC shell / Diameter: 485 Å / T number (triangulation number): 1 |
Virus shell | Shell ID: 2 / Name: NC shell / Diameter: 555 Å / T number (triangulation number): 13 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Vitrification | Cryogen name: ETHANE |
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-Electron microscopy
Microscope | FEI TECNAI F20 |
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Temperature | Average: 93 K |
Alignment procedure | Legacy - Astigmatism: objective lens astigmatism was corrected at |
Image recording | Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: ZEISS SCAI / Digitization - Sampling interval: 7 µm / Number real images: 52 / Bits/pixel: 12 |
Tilt angle min | 0 |
Tilt angle max | 0 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.0 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.4 µm / Nominal magnification: 50000 |
Sample stage | Specimen holder: Side entry liquid nitrogen-cooled cryo specimen holder Specimen holder model: OTHER |
Experimental equipment | Model: Tecnai F20 / Image courtesy: FEI Company |
-Image processing
CTF correction | Details: each particle, full CTF correction |
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Final reconstruction | Applied symmetry - Point group: I (icosahedral) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 7.5 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: P3DR / Number images used: 10463 |