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Yorodumi- EMDB-18346: Complex between the 80a-Sak SSAP and the SaPI2 Stl master regulator -
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Open data
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Basic information
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| Title | Complex between the 80a-Sak SSAP and the SaPI2 Stl master regulator | |||||||||
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Keywords | Annealase / SSAP / Single Strand Annealing / Single Strand Binding / Recombineering / Recombination / SaPI / Bacteriophage / Staphylococcal / Complex / SaPI induction / SaPI2 / Mobile Genetic Element / MGE / PICI / Phage-Inducible Chromosomal Island / Ring / Transcription / Transcriptonal regulator / GENE REGULATION | |||||||||
| Function / homology | Cro/C1-type HTH DNA-binding domain / Helix-turn-helix XRE-family like proteins / Cro/C1-type helix-turn-helix domain / Lambda repressor-like, DNA-binding domain superfamily / DNA binding / : / Helix-turn-helix XRE family protein Function and homology information | |||||||||
| Biological species | Staphylococcus phage 80alpha (virus) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||
Authors | Debiasi-Anders G / Mir-Sanchis I | |||||||||
| Funding support | Sweden, 1 items
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Citation | Journal: Nat Commun / Year: 2025Title: Phage parasites targeting phage homologous recombinases provide antiviral immunity. Authors: Gianluca Debiasi-Anders / Cuncun Qiao / Amrita Salim / Na Li / Ignacio Mir-Sanchis / ![]() Abstract: Bacteria often carry multiple genes encoding anti-phage defense systems, clustered in defense islands and phage satellites. Various unrelated anti-phage defense systems target phage-encoded ...Bacteria often carry multiple genes encoding anti-phage defense systems, clustered in defense islands and phage satellites. Various unrelated anti-phage defense systems target phage-encoded homologous recombinases (HRs) through unclear mechanisms. Here, we show that the phage satellite SaPI2, which does not encode orthodox anti-phage defense systems, provides antiviral immunity mediated by Stl2, the SaPI2-encoded transcriptional repressor. Stl2 targets and inhibits phage-encoded HRs, including Sak and Sak4, two HRs from the Rad52-like and Rad51-like superfamilies. Remarkably, apo Stl2 forms a collar of dimers oligomerizing as closed rings and as filaments, mimicking the quaternary structure of its targets. Stl2 decorates both Sak rings and Sak4 filaments. The oligomerization of Stl2 as a collar of dimers is necessary for its inhibitory activity both in vitro and in vivo. Our results shed light on the mechanisms underlying antiviral immunity against phages carrying divergent HRs. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_18346.map.gz | 239.7 MB | EMDB map data format | |
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| Header (meta data) | emd-18346-v30.xml emd-18346.xml | 20.4 KB 20.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_18346_fsc.xml | 16.7 KB | Display | FSC data file |
| Images | emd_18346.png | 184.6 KB | ||
| Masks | emd_18346_msk_1.map | 476.8 MB | Mask map | |
| Filedesc metadata | emd-18346.cif.gz | 6.6 KB | ||
| Others | emd_18346_half_map_1.map.gz emd_18346_half_map_2.map.gz | 441.5 MB 441.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18346 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18346 | HTTPS FTP |
-Validation report
| Summary document | emd_18346_validation.pdf.gz | 164.7 KB | Display | EMDB validaton report |
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| Full document | emd_18346_full_validation.pdf.gz | 164.3 KB | Display | |
| Data in XML | emd_18346_validation.xml.gz | 572 B | Display | |
| Data in CIF | emd_18346_validation.cif.gz | 483 B | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18346 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18346 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8qe9MC ![]() 8pq8C ![]() 8q86C ![]() 8rc5C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_18346.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.704 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_18346_msk_1.map | ||||||||||||
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-Half map: #2
| File | emd_18346_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_18346_half_map_2.map | ||||||||||||
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Sample components
-Entire : Complex between the 80a-Sak SSAP and the SaPI2 Stl master regulator
| Entire | Name: Complex between the 80a-Sak SSAP and the SaPI2 Stl master regulator |
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| Components |
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-Supramolecule #1: Complex between the 80a-Sak SSAP and the SaPI2 Stl master regulator
| Supramolecule | Name: Complex between the 80a-Sak SSAP and the SaPI2 Stl master regulator type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Molecular weight | Theoretical: 1.6 MDa |
-Supramolecule #2: 80a-Sak SSAP
| Supramolecule | Name: 80a-Sak SSAP / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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| Source (natural) | Organism: Staphylococcus phage 80alpha (virus) |
-Supramolecule #3: SaPI2 Stl master regulator
| Supramolecule | Name: SaPI2 Stl master regulator / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: DUF1071 domain-containing protein
| Macromolecule | Name: DUF1071 domain-containing protein / type: protein_or_peptide / ID: 1 / Number of copies: 34 / Enantiomer: LEVO |
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| Source (natural) | Organism: Staphylococcus phage 80alpha (virus) |
| Molecular weight | Theoretical: 23.63935 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: TEQTLFEQLN SKNVNDHTEQ KNGLTYLAWS YAHQELKKID PNYTVKVHEF PHPDINTENY FVPYLATPEG YFVQVSVTVK DSTETEWLP VLDFRNKSLA KGSATTFDIN KAQKRCFVKA SALHGLGLYI YNGEELPSAS DNDITELEER INQFVNLSQE K GRDATIDK ...String: TEQTLFEQLN SKNVNDHTEQ KNGLTYLAWS YAHQELKKID PNYTVKVHEF PHPDINTENY FVPYLATPEG YFVQVSVTVK DSTETEWLP VLDFRNKSLA KGSATTFDIN KAQKRCFVKA SALHGLGLYI YNGEELPSAS DNDITELEER INQFVNLSQE K GRDATIDK TMRWLKISNI NKLSQKQIAE AHQKLDAGLK QLDSEEKQ UniProtKB: UNIPROTKB: A0A0E1VL05 |
-Macromolecule #2: Helix-turn-helix XRE family protein
| Macromolecule | Name: Helix-turn-helix XRE family protein / type: protein_or_peptide / ID: 2 / Number of copies: 30 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 27.148473 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGIRNRLSEL LSERGLKISR VAKDVKIARS SLTSMAQNDS EMIRYDAIDK LCSYLHISPS EFFEHNPINF DFTFDEEPNY KINDVFEGF EVTANITHAF SIENFDFEIL VDVELDNRQK LNFDLDVSYK ETEKITNSQH RFIFTIKNED ENIGLKKYVD S LSAGLKNL ...String: MGIRNRLSEL LSERGLKISR VAKDVKIARS SLTSMAQNDS EMIRYDAIDK LCSYLHISPS EFFEHNPINF DFTFDEEPNY KINDVFEGF EVTANITHAF SIENFDFEIL VDVELDNRQK LNFDLDVSYK ETEKITNSQH RFIFTIKNED ENIGLKKYVD S LSAGLKNL LFKKINQKLS GYVSEIIVKN IDDIEELFPN KGEKSTTLHK EILQTDSRLS SDIFKEYGSH HHHHH UniProtKB: Helix-turn-helix XRE family protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8.1 Component:
Details: 20mM Tris-HCl pH 7.6, 100mM NaCl, 1mM DTT | ||||||||||||
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| Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||
| 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: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Chain ID: A / Chain - Initial model type: in silico model |
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| Refinement | Space: REAL / Protocol: RIGID BODY FIT |
| Output model | ![]() PDB-8qe9: |
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About Yorodumi



Keywords
Staphylococcus phage 80alpha (virus)
Authors
Sweden, 1 items
Citation











Z (Sec.)
Y (Row.)
X (Col.)












































FIELD EMISSION GUN

