+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-16566 | |||||||||
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Title | 70S-PHIKZ014 PHIKZ phage protein occupied ribosome | |||||||||
Map data | ||||||||||
Sample |
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Keywords | PHIKZ / Phage / hijacked / bacterial / Pseudomonas / PHIKZ014 / ribosome / 5S rRNA | |||||||||
Function / homology | Function and homology information ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / ribosomal small subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / large ribosomal subunit / cytoplasmic translation / small ribosomal subunit / 5S rRNA binding / cytosolic large ribosomal subunit ...ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / ribosomal small subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / large ribosomal subunit / cytoplasmic translation / small ribosomal subunit / 5S rRNA binding / cytosolic large ribosomal subunit / transferase activity / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / RNA binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Pseudomonas aeruginosa PAO1H2O (bacteria) / Pseudomonas aeruginosa PAO1 (bacteria) / Pseudomonas phage phiKZ (virus) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Gerovac M / Vogel J | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nat Microbiol / Year: 2024 Title: Phage proteins target and co-opt host ribosomes immediately upon infection. Authors: Milan Gerovac / Kotaro Chihara / Laura Wicke / Bettina Böttcher / Rob Lavigne / Jörg Vogel / Abstract: Bacteriophages must seize control of the host gene expression machinery to replicate. To bypass bacterial anti-phage defence systems, this host takeover occurs immediately upon infection. A general ...Bacteriophages must seize control of the host gene expression machinery to replicate. To bypass bacterial anti-phage defence systems, this host takeover occurs immediately upon infection. A general understanding of phage mechanisms for immediate targeting of host transcription and translation processes is lacking. Here we introduce an integrative high-throughput approach to uncover phage-encoded proteins that target the gene expression machinery of Pseudomonas aeruginosa immediately upon infection with the jumbo phage ΦKZ. By integrating biochemical, genetic and structural analyses, we identify an abundant and conserved phage factor ΦKZ014 that targets the large ribosomal subunit by binding the 5S ribosomal RNA, and rapidly promotes replication in several clinical isolates. ΦKZ014 is among the earliest ΦKZ proteins expressed after infection and remains bound to ribosomes during the entire translation cycle. Our study provides a strategy to decipher molecular components of phage-mediated host takeover and argues that phage genomes represent an untapped discovery space for proteins that modulate the host gene expression machinery. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_16566.map.gz | 332.3 MB | EMDB map data format | |
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Header (meta data) | emd-16566-v30.xml emd-16566.xml | 83.7 KB 83.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_16566_fsc.xml | 16.9 KB | Display | FSC data file |
Images | emd_16566.png | 129.7 KB | ||
Filedesc metadata | emd-16566.cif.gz | 14.7 KB | ||
Others | emd_16566_additional_1.map.gz emd_16566_additional_2.map.gz emd_16566_half_map_1.map.gz emd_16566_half_map_2.map.gz | 381.3 MB 340.2 MB 361.7 MB 361.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16566 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16566 | HTTPS FTP |
-Related structure data
Related structure data | 8cd1MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_16566.map.gz / Format: CCP4 / Size: 512 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: 1.0635 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: 70S-PHIKZ014 focused
File | emd_16566_additional_1.map | ||||||||||||
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Annotation | 70S-PHIKZ014 focused | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: 70S-tRNA(E)-PHIKZ014
File | emd_16566_additional_2.map | ||||||||||||
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Annotation | 70S-tRNA(E)-PHIKZ014 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_16566_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: 70S-tRNA(P)-PHIKZ014
File | emd_16566_half_map_2.map | ||||||||||||
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Annotation | 70S-tRNA(P)-PHIKZ014 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 70S-PHIKZ014 PHIKZ phage hijacked ribosome
+Supramolecule #1: 70S-PHIKZ014 PHIKZ phage hijacked ribosome
+Macromolecule #1: 50S ribosomal protein L32
+Macromolecule #2: 50S ribosomal protein L34
+Macromolecule #3: 50S ribosomal protein L35
+Macromolecule #4: 50S ribosomal protein L36
+Macromolecule #7: 50S ribosomal protein L2
+Macromolecule #8: 50S ribosomal protein L3
+Macromolecule #10: 50S ribosomal protein L4
+Macromolecule #11: 50S ribosomal protein L5
+Macromolecule #12: 50S ribosomal protein L6
+Macromolecule #13: 50S ribosomal protein L9
+Macromolecule #14: 50S ribosomal protein L13
+Macromolecule #15: 50S ribosomal protein L14
+Macromolecule #16: 50S ribosomal protein L15
+Macromolecule #17: 50S ribosomal protein L31
+Macromolecule #18: 50S ribosomal protein L16
+Macromolecule #19: 50S ribosomal protein L17
+Macromolecule #20: 50S ribosomal protein L18
+Macromolecule #21: 50S ribosomal protein L19
+Macromolecule #22: 50S ribosomal protein L20
+Macromolecule #23: 50S ribosomal protein L21
+Macromolecule #24: Large ribosomal subunit protein uL22
+Macromolecule #25: 50S ribosomal protein L23
+Macromolecule #26: 50S ribosomal protein L24
+Macromolecule #27: 50S ribosomal protein L25
+Macromolecule #28: 50S ribosomal protein L27
+Macromolecule #29: 50S ribosomal protein L28
+Macromolecule #30: 50S ribosomal protein L29
+Macromolecule #31: 50S ribosomal protein L30
+Macromolecule #33: 30S ribosomal protein S2
+Macromolecule #34: 30S ribosomal protein S3
+Macromolecule #35: 30S ribosomal protein S4
+Macromolecule #36: 30S ribosomal protein S5
+Macromolecule #37: 30S ribosomal protein S6
+Macromolecule #38: 30S ribosomal protein S7
+Macromolecule #39: 30S ribosomal protein S8
+Macromolecule #40: 30S ribosomal protein S9
+Macromolecule #41: 30S ribosomal protein S10
+Macromolecule #42: 30S ribosomal protein S11
+Macromolecule #43: 30S ribosomal protein S12
+Macromolecule #44: 30S ribosomal protein S13
+Macromolecule #45: 30S ribosomal protein S14
+Macromolecule #46: 30S ribosomal protein S15
+Macromolecule #47: 30S ribosomal protein S16
+Macromolecule #48: 30S ribosomal protein S17
+Macromolecule #49: 30S ribosomal protein S18
+Macromolecule #50: 30S ribosomal protein S19
+Macromolecule #51: 30S ribosomal protein S20
+Macromolecule #52: 30S ribosomal protein S21
+Macromolecule #53: PHIKZ014
+Macromolecule #5: 23S rRNA
+Macromolecule #6: 5S rRNA
+Macromolecule #9: tRNA
+Macromolecule #32: 16S rRNA
+Macromolecule #54: MAGNESIUM ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 Details: 20 mM HEPES/KOH pH 7.5, 150 mM KCl, 16 mM MgCl2, 1 mM DTT, 0.1% TritonX100 |
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Grid | Model: Quantifoil R3/3 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 0.2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Pretreatment - Atmosphere: OTHER |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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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 FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 5.0 µm / Nominal defocus min: 1.2 µm |
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Number real images: 8431 / Average exposure time: 5.16 sec. / Average electron dose: 88.28 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Protocol: AB INITIO MODEL |
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Output model | PDB-8cd1: |