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Open data
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Basic information
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Title | C3 reconstruction of extended phiCD508 needle | |||||||||
![]() | Extended phiCD508 needle sharpened map (Bfactor = -103.9A) | |||||||||
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![]() | Bacteriophage / virus / needle / baseplate | |||||||||
Function / homology | ![]() virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / viral tail assembly / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.96 Å | |||||||||
![]() | Wilson JS / Fagan RP / Bullough PA | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular mechanism of bacteriophage contraction structure of an S-layer-penetrating bacteriophage. Authors: Jason S Wilson / Louis-Charles Fortier / Robert P Fagan / Per A Bullough / ![]() ![]() Abstract: The molecular details of phage tail contraction and bacterial cell envelope penetration remain poorly understood and are completely unknown for phages infecting bacteria enveloped by proteinaceous S- ...The molecular details of phage tail contraction and bacterial cell envelope penetration remain poorly understood and are completely unknown for phages infecting bacteria enveloped by proteinaceous S-layers. Here, we reveal the extended and contracted atomic structures of an intact contractile-tailed phage (φCD508) that binds to and penetrates the protective S-layer of the Gram-positive human pathogen The tail is unusually long (225 nm), and it is also notable that the tail contracts less than those studied in related contractile injection systems such as the model phage T4 (∼20% compared with ∼50%). Surprisingly, we find no evidence of auxiliary enzymatic domains that other phages exploit in cell wall penetration, suggesting that sufficient energy is released upon tail contraction to penetrate the S-layer and the thick cell wall without enzymatic activity. Instead, the unusually long tail length, which becomes more flexible upon contraction, likely contributes toward the required free energy release for envelope penetration. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 265.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 25.8 KB 25.8 KB | Display Display | ![]() |
Images | ![]() | 43.6 KB | ||
Filedesc metadata | ![]() | 8.1 KB | ||
Others | ![]() ![]() | 382.1 MB 380.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9g8sMC ![]() 9gayC ![]() 9gazC ![]() 9gb0C ![]() 9gb1C ![]() 9gb2C ![]() 9gb3C ![]() 9gb4C ![]() 9gb5C ![]() 9gb6C ![]() 9gb7C ![]() 9gb8C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Extended phiCD508 needle sharpened map (Bfactor = -103.9A) | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: extended phiCD508 needle Half map A
File | emd_51138_half_map_1.map | ||||||||||||
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Annotation | extended phiCD508 needle Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: extended phiCD508 needle Half map B
File | emd_51138_half_map_2.map | ||||||||||||
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Annotation | extended phiCD508 needle Half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Extended phiCD508 needle complex
+Supramolecule #1: Extended phiCD508 needle complex
+Macromolecule #1: Baseplate J family protein
+Macromolecule #2: XkdT-related protein
+Macromolecule #3: Peptidoglycan-binding LysM protein
+Macromolecule #4: XkdM-related protein
+Macromolecule #5: Tail sheath
+Macromolecule #6: XkdS-related protein
+Macromolecule #7: Phage protein
+Macromolecule #8: XkdQ-related protein
+Macromolecule #9: Tail tape measure
+Macromolecule #10: FE (II) ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 42.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 81000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Applied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.96 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 17759 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |