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Open data
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Basic information
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Title | The structure of Microviridae PJNS001 | |||||||||
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![]() | structual proteins / VIRUS | |||||||||
Function / homology | ![]() symbiont-mediated perturbation of host process / T=1 icosahedral viral capsid / viral capsid / host cell cytoplasm / symbiont entry into host cell / virion attachment to host cell / structural molecule activity / DNA binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.68 Å | |||||||||
![]() | Hu WL / Chen YB / Wei YM / Gao Y | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Structural basis for Salmonella infection by two Microviridae phages. Authors: Wanlong Hu / Zhengjie Liu / Yuming Wei / Qucheng Bian / Weiqi Lan / Chongzheng Fan / Jiaoyang Song / Qianqian Sun / Xiaojie Zhang / Yuqing Liu / Yan Gao / Yibao Chen / ![]() Abstract: The global resurgence of multidrug-resistant Salmonella species, responsible for millions of annual infections, underscores the urgent need for alternative antimicrobial strategies, such as phage ...The global resurgence of multidrug-resistant Salmonella species, responsible for millions of annual infections, underscores the urgent need for alternative antimicrobial strategies, such as phage therapy. Microviridae phages offer a promising model for studying phage-host interactions with their unique structural and infection mechanisms. Here, we identify two Microviridae phages, PJNS001 and PJNS002, with different host receptor dependencies, and determine their cryo-EM structures at 2.68 Å and 2.59 Å resolution, respectively. These icosahedral capsids with T = 1 symmetry exhibit a unique vertex reinforcement mechanism, stabilizing the viral assembly. The specific pentameric adaptations, coupled with DNA binding protein engagements and thermodynamic constraints, collectively preclude the formation of hybrid virions. Structural analysis and in situ visualization reveal spike protein features and host-attachment intermediates, informing host specificity. Together, these findings advance our understanding of Microviridae infection mechanisms and provide a structural framework for rational phage design against antibiotic-resistant pathogens. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 229.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.5 KB 24.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.1 KB | Display | ![]() |
Images | ![]() | 201.8 KB | ||
Filedesc metadata | ![]() | 6.9 KB | ||
Others | ![]() ![]() | 223.9 MB 223.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 22.5 KB | Display | |
Data in CIF | ![]() | 29 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9k3mMC ![]() 9k3nC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_62019_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_62019_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Microviridae
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Microviridae
Supramolecule | Name: Microviridae / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: T=1 icosahedral virus / NCBI-ID: 10841 / Sci species name: Microviridae / Sci species strain: PJNS001 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: Yes |
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Host (natural) | Organism: ![]() |
Molecular weight | Theoretical: 4.31 MDa |
Virus shell | Shell ID: 1 / Diameter: 290.0 Å / T number (triangulation number): 1 |
-Macromolecule #1: Capsid protein F
Macromolecule | Name: Capsid protein F / type: protein_or_peptide / ID: 1 / Number of copies: 60 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 48.50048 KDa |
Sequence | String: MSNVQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIKFMKDG VNAAPLPTVN TTGYIDHAAF LGTINPDTNK IPKHLFQGYL NIYNNYFKAP WMPDRTEANP NQLNEDDARY G FRCCHLKN ...String: MSNVQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIKFMKDG VNAAPLPTVN TTGYIDHAAF LGTINPDTNK IPKHLFQGYL NIYNNYFKAP WMPDRTEANP NQLNEDDARY G FRCCHLKN IWTAPLPPET ELSRQMTTST TSIDIMGLQA AYANLHTDQE RDYFMQRYRD VISSFGGKTS YDADNRPLLV MR SNFWASG YDVDGTDQTS LGQFSGRVQQ TYKHSVPRFF VPEHGTMFTL ALVRFPPTAT KEIQYLNAKG ALTYTDIAGD PAL YGNLPP REISMKDVFR SGDASKKFKI AEGQWYRYAP SYVSPAYHLL EGFPFIQEPP SGDLQERVLI RHHDYDQCFQ SVQL LQWNS QVKFNVTVYR NLPTTRDSIM TS UniProtKB: Capsid protein F |
-Macromolecule #2: Major spike protein G
Macromolecule | Name: Major spike protein G / type: protein_or_peptide / ID: 2 / Number of copies: 60 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 19.112695 KDa |
Sequence | String: MFQTFISRHN SNFFSDKLVA TSVTPASLAP VLQTPKAASS TLYFNQLTVN AGNGGFLHCI QMDTSVNAAN QVVSVGADIA FDADPKFFA CLVRFESASV PTTLPTDYDV YPLDGRHDGG YYTVKDCVTI DVLPREPGNN VYVGFMVWSN FTATKCRGLV S LNQVIKEI ICLQPLK UniProtKB: Major spike protein G |
-Macromolecule #3: DNA-binding protein J
Macromolecule | Name: DNA-binding protein J / type: protein_or_peptide / ID: 3 / Number of copies: 60 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 4.239017 KDa |
Sequence | String: MSKGKKRSGA RPGRPQPLRG TKGKRKGARL WYVGGQQF UniProtKB: DNA-binding protein J |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 Component:
Details: pH 7.2~7.6 | |||||||||||||||
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: OTHER | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number real images: 4808 / Average exposure time: 1.25 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 3.0 µm / Calibrated defocus min: 0.4 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 22500 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT / Overall B value: 15.89 |
Output model | ![]() PDB-9k3m: |