+Open data
-Basic information
Entry | Database: PDB / ID: 8twc | ||||||
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Title | Acinetobacter phage AP205 T=3 VLP | ||||||
Components | Coat protein | ||||||
Keywords | VIRUS LIKE PARTICLE / Acinetobacter / SsRNA phage virus / VIRUS / VLP | ||||||
Function / homology | viral capsid / Coat protein Function and homology information | ||||||
Biological species | Acinetobacter phage AP205 (virus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||
Authors | Meng, R. / Xing, Z. / Zhang, J. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2024 Title: Structural basis of Acinetobacter type IV pili targeting by an RNA virus. Authors: Ran Meng / Zhongliang Xing / Jeng-Yih Chang / Zihao Yu / Jirapat Thongchol / Wen Xiao / Yuhang Wang / Karthik Chamakura / Zhiqi Zeng / Fengbin Wang / Ry Young / Lanying Zeng / Junjie Zhang / Abstract: Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. ...Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. Single-stranded RNA bacteriophages target the bacterial retractile pili, including type IV. Our study delves into the interaction between Acinetobacter phage AP205 and type IV pili. Using cryo-electron microscopy, we solve structures of the AP205 virion with an asymmetric dimer of maturation proteins, the native Acinetobacter type IV pili bearing a distinct post-translational pilin cleavage, and the pili-bound AP205 showing its maturation proteins adapted to pilin modifications, allowing each phage to bind to one or two pili. Leveraging these results, we develop a 20-kilodalton AP205-derived protein scaffold targeting type IV pili in situ, with potential for research and diagnostics. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8twc.cif.gz | 3.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8twc.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8twc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8twc_validation.pdf.gz | 2.1 MB | Display | wwPDB validaton report |
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Full document | 8twc_full_validation.pdf.gz | 2.3 MB | Display | |
Data in XML | 8twc_validation.xml.gz | 496.7 KB | Display | |
Data in CIF | 8twc_validation.cif.gz | 799.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tw/8twc ftp://data.pdbj.org/pub/pdb/validation_reports/tw/8twc | HTTPS FTP |
-Related structure data
Related structure data | 41666MC 8tobC 8tocC 8tv9C 8tvaC 8tw2C C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 13820.569 Da / Num. of mol.: 180 / Source method: isolated from a natural source / Source: (natural) Acinetobacter phage AP205 (virus) / References: UniProt: Q9AZ42 |
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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: Acinetobacter phage AP205 / Type: VIRUS Details: amplified and purified from infected Acinetobacter GP16 cells. Entity ID: all / Source: NATURAL | |||||||||||||||
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Molecular weight | Value: 2.48 MDa / Experimental value: NO | |||||||||||||||
Source (natural) | Organism: Acinetobacter phage AP205 (virus) | |||||||||||||||
Details of virus | Empty: NO / Enveloped: YES / Isolate: SPECIES / Type: VIRION | |||||||||||||||
Natural host | Organism: Acinetobacter genomosp. 16BJ | |||||||||||||||
Virus shell | Name: Coat / Diameter: 300 nm / Triangulation number (T number): 3 | |||||||||||||||
Buffer solution | pH: 8 / Details: 20mM Tris-HCl, 150mM NaCl, pH 8.0 | |||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: AP205 virion particle | |||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K / Details: 3uL sample applied to a 300-mesh 2/1 copper grid |
-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: 130000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 50 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 10000 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT | ||||||||||||||||||||||||
Refine LS restraints |
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