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Yorodumi- EMDB-4136: Structure of the mammalian rescue complex with Pelota and Hbs1l a... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-4136 | ||||||||||||
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| Title | Structure of the mammalian rescue complex with Pelota and Hbs1l assembled on a polyadenylated mRNA. | ||||||||||||
Map data | Postprocessed, sharpened map. | ||||||||||||
Sample |
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Keywords | Translation / Elongation / Ribosome | ||||||||||||
| Function / homology | Function and homology informationnucleoside-triphosphatase regulator activity / stalled ribosome sensor activity / RNA surveillance / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / mRNA decay by 3' to 5' exoribonuclease / nuclear-transcribed mRNA catabolic process, non-stop decay / mesenchymal to epithelial transition / endoderm development / positive regulation of BMP signaling pathway ...nucleoside-triphosphatase regulator activity / stalled ribosome sensor activity / RNA surveillance / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / mRNA decay by 3' to 5' exoribonuclease / nuclear-transcribed mRNA catabolic process, non-stop decay / mesenchymal to epithelial transition / endoderm development / positive regulation of BMP signaling pathway / ribosomal subunit / ribosome disassembly / inner cell mass cell proliferation / nonfunctional rRNA decay / stem cell population maintenance / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / 90S preribosome / chromosome organization / translation elongation factor activity / phagocytic cup / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / translation regulator activity / gastrulation / MDM2/MDM4 family protein binding / cytosolic ribosome / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / rescue of stalled ribosome / DNA-(apurinic or apyrimidinic site) lyase / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / positive regulation of apoptotic signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / spindle / rRNA processing / antimicrobial humoral immune response mediated by antimicrobial peptide / rhythmic process / positive regulation of canonical Wnt signaling pathway / large ribosomal subunit / regulation of translation / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / perikaryon / defense response to Gram-negative bacterium / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / killing of cells of another organism / cytosolic large ribosomal subunit / cytoplasmic translation / cell differentiation / tRNA binding / mitochondrial inner membrane / postsynaptic density / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / GTPase activity / mRNA binding / apoptotic process / dendrite / synapse / centrosome / GTP binding / nucleolus / perinuclear region of cytoplasm / endoplasmic reticulum / Golgi apparatus / signal transduction / DNA binding / RNA binding / extracellular exosome / zinc ion binding / metal ion binding / nucleus / membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||
| Biological species | ![]() Homo sapiens (human) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.99 Å | ||||||||||||
Authors | Shao S / Murray J | ||||||||||||
| Funding support | United Kingdom, 3 items
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Citation | Journal: Cell / Year: 2016Title: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes. Authors: Sichen Shao / Jason Murray / Alan Brown / Jack Taunton / V Ramakrishnan / Ramanujan S Hegde / ![]() Abstract: In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the ...In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factor⋅GTPase complexes representing intermediates of translation elongation (aminoacyl-tRNA⋅eEF1A), termination (eRF1⋅eRF3), and ribosome rescue (Pelota⋅Hbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factor⋅GTPase complex to ensure translational fidelity. | ||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_4136.map.gz | 13.5 MB | EMDB map data format | |
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| Header (meta data) | emd-4136-v30.xml emd-4136.xml | 106 KB 106 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_4136_fsc.xml | 14.6 KB | Display | FSC data file |
| Images | emd_4136.png | 189 KB | ||
| Filedesc metadata | emd-4136.cif.gz | 21.4 KB | ||
| Others | emd_4136_half_map_1.map.gz emd_4136_half_map_2.map.gz | 247.8 MB 248.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4136 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4136 | HTTPS FTP |
-Validation report
| Summary document | emd_4136_validation.pdf.gz | 421.2 KB | Display | EMDB validaton report |
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| Full document | emd_4136_full_validation.pdf.gz | 420.3 KB | Display | |
| Data in XML | emd_4136_validation.xml.gz | 20.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4136 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4136 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5lzyMC ![]() 4129C ![]() 4130C ![]() 4131C ![]() 4132C ![]() 4133C ![]() 4134C ![]() 4135C ![]() 4137C ![]() 5lzsC ![]() 5lztC ![]() 5lzuC ![]() 5lzvC ![]() 5lzwC ![]() 5lzxC ![]() 5lzzC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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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_4136.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Postprocessed, sharpened map. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: Half map 1.
| File | emd_4136_half_map_1.map | ||||||||||||
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| Annotation | Half map 1. | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map 2.
| File | emd_4136_half_map_2.map | ||||||||||||
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| Annotation | Half map 2. | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Affinity-purified 80S ribosome-nascent chain complex reconstitute...
+Supramolecule #1: Affinity-purified 80S ribosome-nascent chain complex reconstitute...
+Macromolecule #1: uL2
+Macromolecule #2: uL3
+Macromolecule #3: uL4
+Macromolecule #4: 60S ribosomal protein L5
+Macromolecule #5: 60S ribosomal protein L6
+Macromolecule #6: uL30
+Macromolecule #7: eL8
+Macromolecule #8: uL6
+Macromolecule #9: Ribosomal protein L10 (Predicted)
+Macromolecule #10: uL5
+Macromolecule #11: eL13
+Macromolecule #12: eL14
+Macromolecule #13: Ribosomal protein L15
+Macromolecule #14: uL13
+Macromolecule #15: uL22
+Macromolecule #16: eL18
+Macromolecule #17: eL19
+Macromolecule #18: eL20
+Macromolecule #19: eL21
+Macromolecule #20: eL22
+Macromolecule #21: eL14
+Macromolecule #22: eL24
+Macromolecule #23: eL23
+Macromolecule #24: uL24
+Macromolecule #25: 60S ribosomal protein L27
+Macromolecule #26: uL15
+Macromolecule #27: eL29
+Macromolecule #28: eL30
+Macromolecule #29: eL31
+Macromolecule #30: eL32
+Macromolecule #31: eL33
+Macromolecule #32: eL34
+Macromolecule #33: uL29
+Macromolecule #34: 60S ribosomal protein L36
+Macromolecule #35: eL37
+Macromolecule #36: eL38
+Macromolecule #37: eL39
+Macromolecule #38: eL40
+Macromolecule #39: eL41
+Macromolecule #40: eL42
+Macromolecule #41: eL43
+Macromolecule #42: eL28
+Macromolecule #43: uL10
+Macromolecule #44: uL11
+Macromolecule #50: uS2
+Macromolecule #51: 40S ribosomal protein S3a
+Macromolecule #52: uS5
+Macromolecule #53: uS3
+Macromolecule #54: eS4
+Macromolecule #55: uS7
+Macromolecule #56: 40S ribosomal protein S6
+Macromolecule #57: eS7
+Macromolecule #58: eS8
+Macromolecule #59: Ribosomal protein S9 (Predicted)
+Macromolecule #60: eS10
+Macromolecule #61: uS17
+Macromolecule #62: 40S ribosomal protein S12
+Macromolecule #63: uS15
+Macromolecule #64: uS11
+Macromolecule #65: uS19
+Macromolecule #66: uS9
+Macromolecule #67: eS17
+Macromolecule #68: uS13
+Macromolecule #69: eS19
+Macromolecule #70: uS10
+Macromolecule #71: eS21
+Macromolecule #72: uS8
+Macromolecule #73: uS12
+Macromolecule #74: eS24
+Macromolecule #75: eS25
+Macromolecule #76: eS26
+Macromolecule #77: 40S ribosomal protein S27
+Macromolecule #78: eS28
+Macromolecule #79: uS14
+Macromolecule #80: eS30
+Macromolecule #81: eS31
+Macromolecule #82: RACK1
+Macromolecule #84: Protein pelota homolog
+Macromolecule #85: HBS1-like protein
+Macromolecule #45: tRNA
+Macromolecule #46: 28S ribosomal RNA
+Macromolecule #47: 5S ribosomal RNA
+Macromolecule #48: 5.8S ribosomal RNA
+Macromolecule #49: 18S ribosomal RNA
+Macromolecule #83: mRNA (polyadenylated)
+Macromolecule #86: MAGNESIUM ION
+Macromolecule #87: ZINC ION
+Macromolecule #88: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.2 mg/mL | |||||||||||||||
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| Buffer | pH: 7.4 Component:
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| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 5 / Pretreatment - Type: GLOW DISCHARGE | |||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK III Details: 3 ul aliquots were applied to the grid and incubated for 30 s, before blotting for 3s to remove excess solution.. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Number real images: 1112 / Average exposure time: 1.0 sec. / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Calibrated magnification: 104478 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal magnification: 59000 |
| 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
| Refinement | Space: RECIPROCAL / Protocol: OTHER / Overall B value: 63.6 / Target criteria: FSCaverage |
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| Output model | ![]() PDB-5lzy: |
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About Yorodumi


Keywords
Homo sapiens (human)
Authors
United Kingdom, 3 items
Citation
UCSF Chimera





































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