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Yorodumi- PDB-8gmo: Bacteriophage T4 capsid shell containing 9DE insertions into the ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8gmo | ||||||||||||
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Title | Bacteriophage T4 capsid shell containing 9DE insertions into the gp23* major capsid protein subunits | ||||||||||||
Components |
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Keywords | VIRUS LIKE PARTICLE / Bacteriophage T4 / capsid shell / phage display / decorated capsid / phage head | ||||||||||||
Function / homology | Capsid vertex protein / Major capsid protein, Myoviridae / Major capsid protein Gp23 / Capsid protein, T4-like bacteriophage-like / T=13 icosahedral viral capsid / viral capsid / Major capsid protein / Capsid vertex protein Function and homology information | ||||||||||||
Biological species | Tequatrovirus T4 | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||||||||
Authors | Fokine, A. / Rao, V.B. | ||||||||||||
Funding support | United States, 3items
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Citation | Journal: Nat Commun / Year: 2023 Title: Design of bacteriophage T4-based artificial viral vectors for human genome remodeling. Authors: Jingen Zhu / Himanshu Batra / Neeti Ananthaswamy / Marthandan Mahalingam / Pan Tao / Xiaorong Wu / Wenzheng Guo / Andrei Fokine / Venigalla B Rao / Abstract: Designing artificial viral vectors (AVVs) programmed with biomolecules that can enter human cells and carry out molecular repairs will have broad applications. Here, we describe an assembly-line ...Designing artificial viral vectors (AVVs) programmed with biomolecules that can enter human cells and carry out molecular repairs will have broad applications. Here, we describe an assembly-line approach to build AVVs by engineering the well-characterized structural components of bacteriophage T4. Starting with a 120 × 86 nm capsid shell that can accommodate 171-Kbp DNA and thousands of protein copies, various combinations of biomolecules, including DNAs, proteins, RNAs, and ribonucleoproteins, are externally and internally incorporated. The nanoparticles are then coated with cationic lipid to enable efficient entry into human cells. As proof of concept, we assemble a series of AVVs designed to deliver full-length dystrophin gene or perform various molecular operations to remodel human genome, including genome editing, gene recombination, gene replacement, gene expression, and gene silencing. These large capacity, customizable, multiplex, and all-in-one phage-based AVVs represent an additional category of nanomaterial that could potentially transform gene therapies and personalized medicine. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8gmo.cif.gz | 8 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8gmo.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8gmo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gm/8gmo ftp://data.pdbj.org/pub/pdb/validation_reports/gm/8gmo | HTTPS FTP |
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-Related structure data
Related structure data | 40228MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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Symmetry | Point symmetry: (Schoenflies symbol: D5 (2x5 fold dihedral)) |
-Components
#1: Protein | Mass: 49790.727 Da / Num. of mol.: 93 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Tequatrovirus T4 / Gene: gp23 / Production host: Escherichia coli (E. coli) / References: UniProt: P04535 #2: Protein | Mass: 45594.375 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Tequatrovirus T4 / Gene: 24 / Production host: Escherichia coli (E. coli) / References: UniProt: P19896 |
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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: Enterobacteria phage T4 / Type: VIRUS / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Enterobacteria phage T4 (virus) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Details of virus | Empty: YES / Enveloped: NO / Isolate: STRAIN / Type: VIRUS-LIKE PARTICLE |
Natural host | Organism: Escherichia coli |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: PELCO Ultrathin Carbon with Lacey Carbon |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
-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: 64000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 600 nm / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 36 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: D5 (2x5 fold dihedral) | |||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 70340 Details: The reconstruction was performed using RELION 3.1. The map was sharpened with an automatically calculated B-factor of -129 A2 using the RELION post-processing tool. Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: OTHER / Space: REAL | |||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 7VS5 Accession code: 7VS5 / Source name: PDB / Type: experimental model |