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Yorodumi- EMDB-60689: Structure of urea-treated empty bacteriophage T5 connector complex -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-60689 | |||||||||||||||
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Title | Structure of urea-treated empty bacteriophage T5 connector complex | |||||||||||||||
Map data | ||||||||||||||||
Sample |
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Keywords | Complex / VIRAL PROTEIN | |||||||||||||||
Function / homology | symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / Tail tube terminator protein p142 Function and homology information | |||||||||||||||
Biological species | Escherichia phage T5 (virus) | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||||||||
Authors | Peng YN / Liu HR | |||||||||||||||
Funding support | China, 4 items
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Citation | Journal: Int J Mol Sci / Year: 2024 Title: Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection. Authors: Yuning Peng / Huanrong Tang / Hao Xiao / Wenyuan Chen / Jingdong Song / Jing Zheng / Hongrong Liu / Abstract: T5 is a siphophage that has been extensively studied by structural and biochemical methods. However, the complete in situ structures of T5 before and after DNA ejection remain unknown. In this study, ...T5 is a siphophage that has been extensively studied by structural and biochemical methods. However, the complete in situ structures of T5 before and after DNA ejection remain unknown. In this study, we used cryo-electron microscopy (cryo-EM) to determine the structures of mature T5 (a laboratory-adapted, fiberless T5 mutant) and urea-treated empty T5 (lacking the tip complex) at near-atomic resolutions. Atomic models of the head, connector complex, tail tube, and tail tip were built for mature T5, and atomic models of the connector complex, comprising the portal protein pb7, adaptor protein p144, and tail terminator protein p142, were built for urea-treated empty T5. Our findings revealed that the aforementioned proteins did not undergo global conformational changes before and after DNA ejection, indicating that these structural features were conserved among most myophages and siphophages. The present study elucidates the underlying mechanisms of siphophage infection and DNA ejection. | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_60689.map.gz | 115.9 MB | EMDB map data format | |
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Header (meta data) | emd-60689-v30.xml emd-60689.xml | 13.3 KB 13.3 KB | Display Display | EMDB header |
Images | emd_60689.png | 69.5 KB | ||
Filedesc metadata | emd-60689.cif.gz | 4.9 KB | ||
Others | emd_60689_half_map_1.map.gz emd_60689_half_map_2.map.gz | 115.8 MB 115.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-60689 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-60689 | HTTPS FTP |
-Validation report
Summary document | emd_60689_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_60689_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_60689_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | emd_60689_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60689 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60689 | HTTPS FTP |
-Related structure data
Related structure data | 9imhMC 8zviC 9ilpC 9ilvC 9imvC 9inyC 9iozC 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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-Map
File | Download / File: emd_60689.map.gz / Format: CCP4 / Size: 125 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: 1.3 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_60689_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_60689_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Escherichia phage T5
Entire | Name: Escherichia phage T5 (virus) |
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Components |
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-Supramolecule #1: Escherichia phage T5
Supramolecule | Name: Escherichia phage T5 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2695836 / Sci species name: Escherichia phage T5 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: Tail tube terminator protein p142
Macromolecule | Name: Tail tube terminator protein p142 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: Escherichia phage T5 (virus) |
Molecular weight | Theoretical: 18.378643 KDa |
Sequence | String: MDHRTSIAQA MVDRISKQMD GSQPDEYFNN LYGNVSRQTY KFEEIREFPY VAVHIGTETG QYLPSGQQWM FLELPILVYD KEKTDIQEQ LEKLVADIKT VIDTGGNLEY TVSKPNGSTF PCEATDMIIT SVSTDEGLLA PYGLAEINVT VRYQPPRRSL R R UniProtKB: Tail tube terminator protein p142 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 32.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.6 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 76271 |
Initial angle assignment | Type: COMMON LINE |
Final angle assignment | Type: COMMON LINE |