+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-28009 | ||||||||||||
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Title | Pseudomonas chlororaphis phage 201phi2-1 PhuZ Filament | ||||||||||||
Map data | unsharpened and filtered to the FSC0.143 resolution cutoff | ||||||||||||
Sample |
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Keywords | Bacteriophage protein / structural protein / viral tubulin / VIRAL PROTEIN | ||||||||||||
Biological species | Pseudomonas phage 201phi2-1 (virus) | ||||||||||||
Method | subtomogram averaging / cryo EM / Resolution: 26.0 Å | ||||||||||||
Authors | Laughlin TG / Villa E | ||||||||||||
Funding support | United States, 3 items
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Citation | Journal: bioRxiv / Year: 2023 Title: Identifying the core genome of the nucleus-forming bacteriophage family and characterization of phage RAY. Abstract: We recently discovered that some bacteriophages establish a nucleus-like replication compartment (phage nucleus), but the core genes that define nucleus-based phage replication and their phylogenetic ...We recently discovered that some bacteriophages establish a nucleus-like replication compartment (phage nucleus), but the core genes that define nucleus-based phage replication and their phylogenetic distribution were unknown. By studying phages that encode the major phage nucleus protein chimallin, including previously sequenced yet uncharacterized phages, we discovered that chimallin-encoding phages share a set of 72 highly conserved genes encoded within seven distinct gene blocks. Of these, 21 core genes are unique to this group, and all but one of these unique genes encode proteins of unknown function. We propose that phages with this core genome comprise a novel viral family we term Chimalliviridae. Fluorescence microscopy and cryo-electron tomography studies of phage vB_EamM_RAY confirm that many of the key steps of nucleus-based replication encoded in the core genome are conserved among diverse chimalliviruses, and reveal that non-core components can confer intriguing variations on this replication mechanism. For instance, unlike previously studied nucleus-forming phages, RAY doesn't degrade the host genome, and its PhuZ homolog appears to form a five-stranded filament with a lumen. This work expands our understanding of phage nucleus and PhuZ spindle diversity and function, providing a roadmap for identifying key mechanisms underlying nucleus-based phage replication. #1: Journal: Nature / Year: 2022 Title: Architecture and self-assembly of the jumbo bacteriophage nuclear shell. Authors: Laughlin TG / Deep A / Prichard AM / Seitz C / Gu Y / Enustun E / Suslov S / Khanna K / Birkholz EA / Armbruster E / McCammon JA / Amaro RE / Pogliano J / Corbett KD / Villa E | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_28009.map.gz | 49.1 KB | EMDB map data format | |
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Header (meta data) | emd-28009-v30.xml emd-28009.xml | 18.9 KB 18.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_28009_fsc.xml | 1 KB | Display | FSC data file |
Images | emd_28009.png | 25.8 KB | ||
Masks | emd_28009_msk_1.map | 55 KB | Mask map | |
Filedesc metadata | emd-28009.cif.gz | 5.1 KB | ||
Others | emd_28009_half_map_1.map.gz emd_28009_half_map_2.map.gz | 44.9 KB 45.1 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28009 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28009 | HTTPS FTP |
-Validation report
Summary document | emd_28009_validation.pdf.gz | 643.6 KB | Display | EMDB validaton report |
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Full document | emd_28009_full_validation.pdf.gz | 643.2 KB | Display | |
Data in XML | emd_28009_validation.xml.gz | 5.5 KB | Display | |
Data in CIF | emd_28009_validation.cif.gz | 6.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28009 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28009 | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article (ref.) |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_28009.map.gz / Format: CCP4 / Size: 54.7 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | unsharpened and filtered to the FSC0.143 resolution cutoff | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 7.5 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_28009_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_28009_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_28009_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Pseudomonas chlororaphis phage 201phi2-1 PhuZ Filament
Entire | Name: Pseudomonas chlororaphis phage 201phi2-1 PhuZ Filament |
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Components |
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-Supramolecule #1: Pseudomonas chlororaphis phage 201phi2-1 PhuZ Filament
Supramolecule | Name: Pseudomonas chlororaphis phage 201phi2-1 PhuZ Filament type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Pseudomonas phage 201phi2-1 (virus) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | subtomogram averaging |
Aggregation state | cell |
-Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: OTHER / Pretreatment - Pressure: 0.019 kPa / Details: 20 mA in a PELCO EasiGLO |
Vitrification | Cryogen name: ETHANE-PROPANE / Instrument: HOMEMADE PLUNGER |
Details | cell suspension |
-Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average electron dose: 1.8 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 6.0 µm / Nominal defocus min: 4.5 µm / Nominal magnification: 42000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |