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Yorodumi- PDB-5iv7: Cryo-electron microscopy structure of the star-shaped, hubless po... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5iv7 | ||||||
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Title | Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate | ||||||
Components | (Baseplate wedge protein ...) x 8 | ||||||
Keywords | VIRAL PROTEIN / T4 / baseplate / post-attachment / bacteriophage / bacterial virus / star-shaped / hubless / membrane-piercing / cell attachment / infection | ||||||
Function / homology | Function and homology information virus tail, baseplate / viral tail assembly / viral release from host cell / identical protein binding Similarity search - Function | ||||||
Biological species | Enterobacteria phage T4 (virus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.77 Å | ||||||
Authors | Taylor, N.M.I. / Guerrero-Ferreira, R.C. / Goldie, K.N. / Stahlberg, H. / Leiman, P.G. | ||||||
Citation | Journal: Nature / Year: 2016 Title: Structure of the T4 baseplate and its function in triggering sheath contraction. Authors: Nicholas M I Taylor / Nikolai S Prokhorov / Ricardo C Guerrero-Ferreira / Mikhail M Shneider / Christopher Browning / Kenneth N Goldie / Henning Stahlberg / Petr G Leiman / Abstract: Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This ...Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 5iv7.cif.gz | 6.6 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5iv7.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 5iv7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5iv7_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 5iv7_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 5iv7_validation.xml.gz | 856.9 KB | Display | |
Data in CIF | 5iv7_validation.cif.gz | 1.3 MB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iv/5iv7 ftp://data.pdbj.org/pub/pdb/validation_reports/iv/5iv7 | HTTPS FTP |
-Related structure data
Related structure data | 3396MC 3374C 3392C 3393C 3394C 3395C 3397C 5iv5C 5iw9C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
-Baseplate wedge protein ... , 8 types, 96 molecules ABQRghwxBFBGEAEBCSiyCAECDETUjkzAACBCCEDEE...
#1: Protein | Mass: 74492.641 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / References: UniProt: P19060 #2: Protein | Mass: 119336.516 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P19061 #3: Protein | Mass: 38041.668 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P19062 #4: Protein | Mass: 31024.725 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P10927 #5: Protein | Mass: 66281.680 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P10928 #6: Protein | Mass: 23725.523 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P10929 #7: Protein | Mass: 15111.101 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P09425 #8: Protein | Mass: 22990.885 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Enterobacteria phage T4 (virus) / Plasmid details: am18/am23 mutant / References: UniProt: P16011 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Star-shaped, hubless post-attachment T4 baseplate-tail tube complex Type: COMPLEX Details: The short tail fibers (gp12 trimers) appear more flexible, and no special effort was made to reconstruct them. They were partly masked out by the circular mask.The total mass of the ...Details: The short tail fibers (gp12 trimers) appear more flexible, and no special effort was made to reconstruct them. They were partly masked out by the circular mask.The total mass of the reconstructed volume was approximately 4.5 MDa (excluding short tail fibers). The short-tail fibers were not included in the PDB file. Entity ID: all / Source: NATURAL | ||||||||||||||||||||
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Molecular weight | Value: 5.5 MDa / Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: Enterobacteria phage T4 (virus) / Strain: am18/am23 mutant | ||||||||||||||||||||
Buffer solution | pH: 8 | ||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: In addition to hexagonal pre-attachment baseplate-tail tube complexes, the sample also contained some star-shaped, hubless post-attachment baseplates. The current model is that star-shaped, ...Details: In addition to hexagonal pre-attachment baseplate-tail tube complexes, the sample also contained some star-shaped, hubless post-attachment baseplates. The current model is that star-shaped, hubless post-attachment baseplate. | ||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % Details: Applied 3.5 ul of sample and blotting 3 seconds before plunging |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Calibrated magnification: 37700 X / Nominal defocus max: 4000 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm |
Specimen holder | Cryogen: HELIUM / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 80 K / Temperature (min): 80 K |
Image recording | Electron dose: 60 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
EM imaging optics | Energyfilter name: GIF Quantum LS / Energyfilter upper: 20 eV / Energyfilter lower: 0 eV |
Image scans | Movie frames/image: 40 / Used frames/image: 3-40 |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 47516 | |||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C6 (6 fold cyclic) | |||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 6.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5176 / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: OTHER / Space: REAL | |||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 5IV5 |