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Yorodumi- PDB-9mu2: SaPI1 neck structure with DNA, tail completion protein, and tape ... -
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Basic information
| Entry | Database: PDB / ID: 9mu2 | ||||||
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| Title | SaPI1 neck structure with DNA, tail completion protein, and tape measure protein | ||||||
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Keywords | VIRUS LIKE PARTICLE / sapi / capsid / tail / phage | ||||||
| Function / homology | Function and homology information | ||||||
| Biological species | Staphylococcus phage 80alpha (virus) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.54 Å | ||||||
Authors | Kizziah, J.L. / Dokland, T. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Structure / Year: 2025Title: Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein. Authors: James L Kizziah / Amarshi Mukherjee / Laura K Parker / Terje Dokland / ![]() Abstract: The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, ...The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from helper-encoded structural proteins. 80α and SaPI1 virions consist of an icosahedral head connected via a portal vertex to a long, non-contractile tail. A connector or "neck" forms the interface between the tail and the head. Here, we have determined the high-resolution structure of the neck section of SaPI1 virions, including the dodecameric portal and head-tail-connector proteins, and the hexameric head-tail joining, tail terminator and major tail proteins. We also resolved the DNA, the tail completion protein (TCP), and the tape measure protein (TMP) inside the tail, features that have not previously been observed at high resolution. Our study provides insights into the assembly and infection process in this important group of MGEs. #1: Journal: bioRxiv / Year: 2024 Title: Structure of the bacteriophage 80α neck shows the interactions between DNA, tail completion protein and tape measure protein. Authors: James L Kizziah / Amarshi Mukherjee / Laura K Parker / Terje Dokland / ![]() Abstract: Tailed bacteriophages with double-stranded DNA genomes (class ) play an important role in the evolution of bacterial pathogenicity, both as carriers of genes encoding virulence factors and as the ...Tailed bacteriophages with double-stranded DNA genomes (class ) play an important role in the evolution of bacterial pathogenicity, both as carriers of genes encoding virulence factors and as the main means of horizontal transfer of mobile genetic elements (MGEs) in many bacteria, such as . The pathogenicity islands (SaPIs), including SaPI1, are a type of MGEs are that carry a variable complement of genes encoding virulence factors. SaPI1 is mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI1 genome into virions made from structural proteins supplied by the helper. 80α and SaPI1 virions consist of an icosahedral head (capsid) connected via a unique vertex to a long, non-contractile tail. At one end of the tail, proteins associated with the baseplate recognize and bind to the host. At the other end, a connector or "neck" forms the interface between the tail and the head. The neck consists of several specialized proteins with specific roles in DNA packaging, phage assembly, and DNA ejection. Using cryo-electron microscopy and three-dimensional reconstruction, we have determined the high-resolution structure of the neck section of SaPI1 virions made in the presence of phage 80α, including the dodecameric portal (80α gene product (gp) 42) and head-tail-connector (gp49) proteins, the hexameric head-tail joining (gp50) and tail terminator (gp52) proteins, and the major tail protein (gp53) itself. We were also able to resolve the DNA, the tail completion protein (gp51) and the tape measure protein (gp56) inside the tail. This is the first detailed structural description of these features in a bacteriophage, providing insights into the assembly and infection process in this important group of MGEs and their helper bacteriophages. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9mu2.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9mu2.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9mu2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9mu2_validation.pdf.gz | 2.5 MB | Display | wwPDB validaton report |
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| Full document | 9mu2_full_validation.pdf.gz | 2.5 MB | Display | |
| Data in XML | 9mu2_validation.xml.gz | 97.7 KB | Display | |
| Data in CIF | 9mu2_validation.cif.gz | 155.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/9mu2 ftp://data.pdbj.org/pub/pdb/validation_reports/mu/9mu2 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 48617MC ![]() 9mu3C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 6 types, 40 molecules ABGHSTYZefklCIUagmDJVbhnEFKLWX...
| #1: Protein | Mass: 12809.583 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: UniProt: S4V9M2#2: Protein | Mass: 11815.448 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: UniProt: A0AA96SLM5#3: Protein | Mass: 14730.251 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: UniProt: A4ZFB8#4: Protein | Mass: 21551.746 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: UniProt: A4ZFB9#5: Protein | Mass: 125891.977 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: UniProt: A4ZFC2#6: Protein | | Mass: 13482.252 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: UniProt: A0AA96SGB5 |
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-DNA chain , 2 types, 2 molecules QR
| #7: DNA chain | Mass: 13596138.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: GenBank: 148717842 |
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| #8: DNA chain | Mass: 13487673.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 80alpha (virus) / References: GenBank: 148717842 |
-Details
| Has protein modification | N |
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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 |
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Sample preparation
| Component | Name: Staphylococcus phage 80alpha / Type: VIRUS / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: Staphylococcus phage 80alpha (virus) |
| Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRUS-LIKE PARTICLE |
| Buffer solution | pH: 7.8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 700 nm |
| Image recording | Electron dose: 35.26 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.54 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35724 / Symmetry type: POINT |
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About Yorodumi



Staphylococcus phage 80alpha (virus)
United States, 1items
Citation


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FIELD EMISSION GUN