+Open data
-Basic information
Entry | Database: PDB / ID: 7yfz | ||||||
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Title | Cyanophage Pam3 baseplate proteins | ||||||
Components |
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Keywords | VIRAL PROTEIN / baseplate / VIRUS | ||||||
Biological species | uncultured cyanophage (environmental samples) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.19 Å | ||||||
Authors | Yang, F. / Jiang, Y.L. / Zhou, C.Z. | ||||||
Funding support | China, 1items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2023 Title: Fine structure and assembly pattern of a minimal myophage Pam3. Authors: Feng Yang / Yong-Liang Jiang / Jun-Tao Zhang / Jie Zhu / Kang Du / Rong-Cheng Yu / Zi-Lu Wei / Wen-Wen Kong / Ning Cui / Wei-Fang Li / Yuxing Chen / Qiong Li / Cong-Zhao Zhou / Abstract: The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail ...The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail contraction mechanism of myophage remain largely unknown. Here, we present the fine structure of a freshwater cyanophage Pam3, which has an icosahedral capsid of ~680 Å in diameter, connected via a three-section neck to an 840-Å-long contractile tail, ending with a three-module baseplate composed of only six protein components. This simplified baseplate consists of a central hub-spike surrounded by six wedge heterotriplexes, to which twelve tail fibers are covalently attached via disulfide bonds in alternating upward and downward configurations. In vitro reduction assays revealed a putative redox-dependent mechanism of baseplate assembly and tail sheath contraction. These findings establish a minimal myophage that might become a user-friendly chassis phage in synthetic biology. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7yfz.cif.gz | 2.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7yfz.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 7yfz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7yfz_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 7yfz_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 7yfz_validation.xml.gz | 195.2 KB | Display | |
Data in CIF | 7yfz_validation.cif.gz | 316.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yf/7yfz ftp://data.pdbj.org/pub/pdb/validation_reports/yf/7yfz | HTTPS FTP |
-Related structure data
Related structure data | 33802MC 7yfwC 8hdrC 8hdsC 8hdtC 8hdwC M: map data used to model this data C: citing same article (ref.) |
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-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Pam3 baseplate wedge ... , 2 types, 18 molecules ABEFHIKLOPQRCDGJMS
#1: Protein | Mass: 32686.787 Da / Num. of mol.: 12 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) #2: Protein | Mass: 26194.811 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) |
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-Protein , 5 types, 24 molecules Xnopqrabcdefhijklmtuvwxy
#3: Protein | Mass: 13889.669 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) #4: Protein | Mass: 19854.342 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) #5: Protein | Mass: 11724.286 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) #6: Protein | Mass: 25201.736 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) #7: Protein | Mass: 23537.537 Da / Num. of mol.: 3 / Source method: isolated from a natural source Source: (natural) uncultured cyanophage (environmental samples) |
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-Details
Has protein modification | Y |
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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: uncultured cyanophage / Type: VIRUS / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: uncultured cyanophage (environmental samples) |
Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION |
Natural host | Organism: Pseudanabaena mucicola |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 300 K |
-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: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software | Name: RELION / Version: 3.1 / Category: 3D reconstruction |
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CTF correction | Type: PHASE FLIPPING ONLY |
3D reconstruction | Resolution: 3.19 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 45155 / Symmetry type: POINT |