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Yorodumi- EMDB-54141: Cryo-EM map of the collided 80S from the ZAK-bound human disome -
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Open data
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Basic information
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| Title | Cryo-EM map of the collided 80S from the ZAK-bound human disome | |||||||||
Map data | Cryo-EM map of the collided 80S from the ZAK-bound human disome | |||||||||
Sample |
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Keywords | ZAK / collision / RSR / quality control / RIBOSOME | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.35 Å | |||||||||
Authors | Niu S / Beckmann R | |||||||||
| Funding support | European Union, 1 items
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Citation | Journal: Nature / Year: 2025Title: ZAK activation at the collided ribosome. Authors: Vienna L Huso / Shuangshuang Niu / Marco A Catipovic / James A Saba / Timo Denk / Eugene Park / Jingdong Cheng / Otto Berninghausen / Thomas Becker / Rachel Green / Roland Beckmann / ![]() Abstract: Ribosome collisions activate the ribotoxic stress response mediated by the MAP3K ZAK, which in turn regulates cell-fate consequences through downstream phosphorylation of the MAPKs p38 and JNK. ...Ribosome collisions activate the ribotoxic stress response mediated by the MAP3K ZAK, which in turn regulates cell-fate consequences through downstream phosphorylation of the MAPKs p38 and JNK. Despite the critical role of ZAK during cellular stress, a mechanistic and structural understanding of ZAK-ribosome interactions and how these lead to activation remain elusive. Here we combine biochemistry and cryo-electron microscopy to discover distinct ZAK-ribosome interactions required for constitutive recruitment and for activation. We find that upon induction of ribosome collisions, interactions between ZAK and the ribosomal protein RACK1 enable its activation by dimerization of its SAM domains at the collision interface. Furthermore, we discover how this process is negatively regulated by the ribosome-binding protein SERBP1 to prevent constitutive ZAK activation. Characterization of novel SAM variants as well as a known pathogenic variant of the SAM domain of ZAK supports a key role of the SAM domain in regulating kinase activity on and off the ribosome, with some mutants bypassing the ribosome requirement for ZAK activation. Collectively, our data provide a mechanistic blueprint of the kinase activity of ZAK at the collided ribosome interface. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_54141.map.gz | 241 MB | EMDB map data format | |
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| Header (meta data) | emd-54141-v30.xml emd-54141.xml | 12.7 KB 12.7 KB | Display Display | EMDB header |
| Images | emd_54141.png | 197 KB | ||
| Filedesc metadata | emd-54141.cif.gz | 3.9 KB | ||
| Others | emd_54141_half_map_1.map.gz emd_54141_half_map_2.map.gz | 442.9 MB 442.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-54141 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-54141 | HTTPS FTP |
-Validation report
| Summary document | emd_54141_validation.pdf.gz | 937 KB | Display | EMDB validaton report |
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| Full document | emd_54141_full_validation.pdf.gz | 936.6 KB | Display | |
| Data in XML | emd_54141_validation.xml.gz | 18.6 KB | Display | |
| Data in CIF | emd_54141_validation.cif.gz | 22.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-54141 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-54141 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_54141.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Cryo-EM map of the collided 80S from the ZAK-bound human disome | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.1632 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Halfmap A for the collided 80S
| File | emd_54141_half_map_1.map | ||||||||||||
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| Annotation | Halfmap A for the collided 80S | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Halfmap B for the collided 80S
| File | emd_54141_half_map_2.map | ||||||||||||
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| Annotation | Halfmap B for the collided 80S | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : ZAK-bound H. sapiens disome-collided 80S ribosome
| Entire | Name: ZAK-bound H. sapiens disome-collided 80S ribosome |
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| Components |
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-Supramolecule #1: ZAK-bound H. sapiens disome-collided 80S ribosome
| Supramolecule | Name: ZAK-bound H. sapiens disome-collided 80S ribosome / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: Homo sapiens (human) |
-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: 7.5 |
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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: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 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: 3.5 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
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Processing
FIELD EMISSION GUN
