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Yorodumi- EMDB-72693: Cryo-EM map of the in vitro reconstituted RAZR:GP77 complex with ... -
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Open data
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Basic information
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| Title | Cryo-EM map of the in vitro reconstituted RAZR:GP77 complex with AlphaFold-predicted models fitted into the density. | |||||||||
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Keywords | Phage-bacterial defense complex / Abortive infection Ring-Activated Zinc-Finger RNase (RAZR) / RNA BINDING PROTEIN | |||||||||
| Function / homology | Domain of unknown function DUF4145 / Domain of unknown function (DUF4145) / DUF4145 domain-containing protein / : Function and homology information | |||||||||
| Biological species | ![]() Escherichia phage SECphi27 (virus) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Lyu Y / Zhang T / Laub M / Ghanbarpour A | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Nature / Year: 2026Title: Bacterial immune activation via supramolecular assembly with phage triggers. Authors: Tong Zhang / Yifei Lyu / Christina R Beck / Naseer Iqbal / Renee Barbosa / Alireza Ghanbarpour / Michael T Laub / ![]() Abstract: Bacteria use diverse mechanisms to protect themselves against phages. Many antiphage systems form large oligomeric complexes, but how oligomerization is regulated during phage infection remains ...Bacteria use diverse mechanisms to protect themselves against phages. Many antiphage systems form large oligomeric complexes, but how oligomerization is regulated during phage infection remains mostly unknown. Here we demonstrate that the bacterial immunity protein ring-activated zinc-finger RNase (RAZR) assembles into an active, 24-meric ring around the circumference of large ring structures formed by two unrelated phage proteins: a putative recombinase and a portal protein. Each multi-layered, megadalton-scale complex enables RAZR to cleave RNA nonspecifically to inhibit translation and restrict phage propagation. The recognition of unrelated phage proteins that form rings with similar diameters indicates that these proteins not only bind to RAZR but also enforce a geometry crucial to activation. The lack of large ring structures in the host probably prevents auto-immunity and RAZR activation before infection. The infection-triggered oligomerization of RAZR mirrors pathogen-induced oligomerization in eukaryotic innate immune complexes, underscoring a common principle of immunity across biology. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_72693.map.gz | 163.4 MB | EMDB map data format | |
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| Header (meta data) | emd-72693-v30.xml emd-72693.xml | 20.9 KB 20.9 KB | Display Display | EMDB header |
| Images | emd_72693.png | 56.2 KB | ||
| Masks | emd_72693_msk_1.map | 325 MB | Mask map | |
| Filedesc metadata | emd-72693.cif.gz | 6.4 KB | ||
| Others | emd_72693_half_map_1.map.gz emd_72693_half_map_2.map.gz | 301.3 MB 301.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-72693 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-72693 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9y9cMC 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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Map
| File | Download / File: emd_72693.map.gz / Format: CCP4 / Size: 325 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: 1.4863 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_72693_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_72693_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_72693_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : RazR:GP77 complex
| Entire | Name: RazR:GP77 complex |
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| Components |
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-Supramolecule #1: RazR:GP77 complex
| Supramolecule | Name: RazR:GP77 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Gp77
| Macromolecule | Name: Gp77 / type: protein_or_peptide / ID: 1 / Number of copies: 24 / Enantiomer: LEVO |
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| Source (natural) | Organism: Escherichia phage SECphi27 (virus) |
| Molecular weight | Theoretical: 25.47565 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MKLSDQFDKV LPALHKARSL FVKVKKDRQN SHLKNRYATL DSVLDAITPA LMDNELMIMQ DGERIDVSTL RVETTVMHVS GQWVKFYFD IPIVKNDPQG VGSAFTYGRR YSAAAAFGLS QADDDAQIAV KTVNDWKRDI EKCESVGELQ EVLKNAWKSS D AASKQVIR ...String: MKLSDQFDKV LPALHKARSL FVKVKKDRQN SHLKNRYATL DSVLDAITPA LMDNELMIMQ DGERIDVSTL RVETTVMHVS GQWVKFYFD IPIVKNDPQG VGSAFTYGRR YSAAAAFGLS QADDDAQIAV KTVNDWKRDI EKCESVGELQ EVLKNAWKSS D AASKQVIR DHYEKRKAEI EIGGARGFNP AKPKENLASD AVDTPNSEKV KSQSITDFEG SSGHHHHHH UniProtKB: UNIPROTKB: A0AAE8YXX1 |
-Macromolecule #2: DUF4145 domain-containing protein
| Macromolecule | Name: DUF4145 domain-containing protein / type: protein_or_peptide / ID: 2 / Number of copies: 24 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 24.707023 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAEYYPAVFE AEAFNCPHCG VYARQFWRRM YGSARELAQR TTEFRMSTCS HCGDDAYWYD GNMIIPAAGN VELPNPDMPD NCKSDYMEA RSIINLSPKG AAALLRLCLQ KLMVHLGEPG ENINKDIRSL VQKGLPVRIQ QAADICRIVG NQAVHPGEIS L DDDPQLAH ...String: MAEYYPAVFE AEAFNCPHCG VYARQFWRRM YGSARELAQR TTEFRMSTCS HCGDDAYWYD GNMIIPAAGN VELPNPDMPD NCKSDYMEA RSIINLSPKG AAALLRLCLQ KLMVHLGEPG ENINKDIRSL VQKGLPVRIQ QAADICRIVG NQAVHPGEIS L DDDPQLAH GLFKLLNIIV DDRITRPKEI EAMFQSMPEG PRQGIENQDR QAREQQQAAN E UniProtKB: DUF4145 domain-containing protein |
-Macromolecule #3: ZINC ION
| Macromolecule | Name: ZINC ION / type: ligand / ID: 3 / Number of copies: 24 / Formula: ZN |
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| Molecular weight | Theoretical: 65.409 Da |
-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 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Number real images: 11152 / Average electron dose: 47.18 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
| 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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| Output model | ![]() PDB-9y9c: |
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About Yorodumi



Keywords
Escherichia phage SECphi27 (virus)
Authors
United States, 2 items
Citation


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FIELD EMISSION GUN
