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- 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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![]() | 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![]() | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||
![]() | Debiasi-Anders G / Mir-Sanchis I | |||||||||
Funding support | ![]()
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![]() | ![]() Title: 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. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 239.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.4 KB 20.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.7 KB | Display | ![]() |
Images | ![]() | 184.6 KB | ||
Masks | ![]() | 476.8 MB | ![]() | |
Filedesc metadata | ![]() | 6.6 KB | ||
Others | ![]() ![]() | 441.5 MB 441.5 MB | ||
Archive directory | ![]() ![]() | 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 ![]() |
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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: 0.704 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #2
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Density Histograms |
-Half map: #1
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Density Histograms |
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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: ![]() |
-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: ![]() |
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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![]() | 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: ![]() |
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: |