+Open data
-Basic information
Entry | Database: PDB / ID: 6qyd | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of the head in mature bacteriophage phi29 | |||||||||||||||
Components |
| |||||||||||||||
Keywords | VIRUS / bacteriophage / cryo-EM / mature virus | |||||||||||||||
Function / homology | Function and homology information viral capsid, fiber / viral procapsid / T=3 icosahedral viral capsid / symbiont entry into host cell / virion attachment to host cell / identical protein binding Similarity search - Function | |||||||||||||||
Biological species | Bacillus phage phi29 (virus) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||||||||
Authors | Xu, J.W. / Wang, D.H. / Gui, M. / Xiang, Y. | |||||||||||||||
Funding support | China, 4items
| |||||||||||||||
Citation | Journal: Nat Commun / Year: 2019 Title: Structural assembly of the tailed bacteriophage ϕ29. Authors: Jingwei Xu / Dianhong Wang / Miao Gui / Ye Xiang / Abstract: The mature virion of the tailed bacteriophage ϕ29 is an ~33 MDa complex that contains more than 450 subunits of seven structural proteins assembling into a prolate head and a short non-contractile ...The mature virion of the tailed bacteriophage ϕ29 is an ~33 MDa complex that contains more than 450 subunits of seven structural proteins assembling into a prolate head and a short non-contractile tail. Here, we report the near-atomic structures of the ϕ29 pre-genome packaging head (prohead), the mature virion and the genome-emptied virion. Structural comparisons suggest local rotation or oscillation of the head-tail connector upon DNA packaging and release. Termination of the DNA packaging occurs through pressure-dependent correlative positional and conformational changes in the connector. The funnel-shaped tail lower collar attaches the expanded narrow end of the connector and has a 180-Å long, 24-strand β barrel narrow stem tube that undergoes conformational changes upon genome release. The appendages form an interlocked assembly attaching the tail around the collar. The membrane active long loops at the distal end of the tail knob exit during the late stage of infection and form the cone-shaped tip of a largely hydrophobic helix barrel, prepared for membrane penetration. | |||||||||||||||
History |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6qyd.cif.gz | 24.2 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6qyd.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6qyd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6qyd_validation.pdf.gz | 3.4 MB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 6qyd_full_validation.pdf.gz | 3.6 MB | Display | |
Data in XML | 6qyd_validation.xml.gz | 3 MB | Display | |
Data in CIF | 6qyd_validation.cif.gz | 4.7 MB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qy/6qyd ftp://data.pdbj.org/pub/pdb/validation_reports/qy/6qyd | HTTPS FTP |
-Related structure data
Related structure data | 4677MC 4655C 4662C 4678C 4679C 4680C 4681C 4682C 4683C 4684C 4685C 6qvkC 6qx7C 6qyjC 6qymC 6qyyC 6qyzC 6qz0C 6qz9C 6qzfC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
#1: Protein | Mass: 49894.906 Da / Num. of mol.: 235 / Source method: isolated from a natural source / Source: (natural) Bacillus phage phi29 (virus) / References: UniProt: P13849 #2: Protein | Mass: 29642.361 Da / Num. of mol.: 165 / Source method: isolated from a natural source / Source: (natural) Bacillus phage phi29 (virus) / References: UniProt: B3VMP4 |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Bacillus virus phi29 / Type: VIRUS / Entity ID: all / Source: NATURAL |
---|---|
Source (natural) | Organism: Bacillus virus phi29 |
Details of virus | Empty: NO / Enveloped: NO / Isolate: STRAIN / Type: VIRION |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
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 |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING ONLY |
---|---|
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 36730 / Symmetry type: POINT |