+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11439 | |||||||||
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Title | Structure of a yeast ABCE1-bound 48S initiation complex | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Translation / Initiation / Ribosome Recycling / ABC Proteins / RIBOSOME | |||||||||
Function / homology | Function and homology information eukaryotic initiation factor eIF2 binding / formation of translation initiation ternary complex / eukaryotic translation initiation factor 3 complex, eIF3e / eukaryotic translation initiation factor 3 complex, eIF3m / incipient cellular bud site / translation reinitiation / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation complex / multi-eIF complex / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) ...eukaryotic initiation factor eIF2 binding / formation of translation initiation ternary complex / eukaryotic translation initiation factor 3 complex, eIF3e / eukaryotic translation initiation factor 3 complex, eIF3m / incipient cellular bud site / translation reinitiation / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation complex / multi-eIF complex / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) / cytoplasmic translational initiation / eukaryotic 43S preinitiation complex / formation of translation preinitiation complex / ribosome disassembly / eukaryotic 48S preinitiation complex / negative regulation of glucose mediated signaling pathway / negative regulation of translational frameshifting / Negative regulators of DDX58/IFIH1 signaling / positive regulation of translational fidelity / RMTs methylate histone arginines / Protein methylation / mTORC1-mediated signalling / Protein hydroxylation / ribosome-associated ubiquitin-dependent protein catabolic process / GDP-dissociation inhibitor activity / regulation of translational initiation / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nonfunctional rRNA decay / preribosome, small subunit precursor / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / Ribosomal scanning and start codon recognition / Major pathway of rRNA processing in the nucleolus and cytosol / mRNA destabilization / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Formation of a pool of free 40S subunits / regulation of amino acid metabolic process / L13a-mediated translational silencing of Ceruloplasmin expression / ribosomal small subunit binding / 90S preribosome / G-protein alpha-subunit binding / positive regulation of protein kinase activity / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / regulation of translational fidelity / Ub-specific processing proteases / ribosomal subunit export from nucleus / ribosomal small subunit export from nucleus / translation regulator activity / translational termination / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / negative regulation of translational initiation / DNA-(apurinic or apyrimidinic site) endonuclease activity / translation initiation factor binding / translation initiation factor activity / cellular response to amino acid starvation / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / GTPase activator activity / ribosome assembly / rescue of stalled ribosome / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / cytosolic ribosome assembly / small-subunit processome / positive regulation of translation / translational initiation / protein kinase C binding / maintenance of translational fidelity / modification-dependent protein catabolic process / cytoplasmic stress granule / protein tag activity / rRNA processing / ribosomal small subunit biogenesis / double-stranded RNA binding / small ribosomal subunit rRNA binding / ribosome biogenesis / ribosome binding / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / protein ubiquitination / iron ion binding / translation / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / negative regulation of gene expression / mRNA binding / ubiquitin protein ligase binding / nucleolus / GTP binding / protein kinase binding / ATP hydrolysis activity Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.2 Å | |||||||||
Authors | Kratzat H / Mackens-Kiani T | |||||||||
Funding support | Germany, France, 2 items
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Citation | Journal: EMBO J / Year: 2021 Title: A structural inventory of native ribosomal ABCE1-43S pre-initiation complexes. Authors: Hanna Kratzat / Timur Mackens-Kiani / Michael Ameismeier / Mia Potocnjak / Jingdong Cheng / Estelle Dacheux / Abdelkader Namane / Otto Berninghausen / Franz Herzog / Micheline Fromont-Racine ...Authors: Hanna Kratzat / Timur Mackens-Kiani / Michael Ameismeier / Mia Potocnjak / Jingdong Cheng / Estelle Dacheux / Abdelkader Namane / Otto Berninghausen / Franz Herzog / Micheline Fromont-Racine / Thomas Becker / Roland Beckmann / Abstract: In eukaryotic translation, termination and ribosome recycling phases are linked to subsequent initiation of a new round of translation by persistence of several factors at ribosomal sub-complexes. ...In eukaryotic translation, termination and ribosome recycling phases are linked to subsequent initiation of a new round of translation by persistence of several factors at ribosomal sub-complexes. These comprise/include the large eIF3 complex, eIF3j (Hcr1 in yeast) and the ATP-binding cassette protein ABCE1 (Rli1 in yeast). The ATPase is mainly active as a recycling factor, but it can remain bound to the dissociated 40S subunit until formation of the next 43S pre-initiation complexes. However, its functional role and native architectural context remains largely enigmatic. Here, we present an architectural inventory of native yeast and human ABCE1-containing pre-initiation complexes by cryo-EM. We found that ABCE1 was mostly associated with early 43S, but also with later 48S phases of initiation. It adopted a novel hybrid conformation of its nucleotide-binding domains, while interacting with the N-terminus of eIF3j. Further, eIF3j occupied the mRNA entry channel via its ultimate C-terminus providing a structural explanation for its antagonistic role with respect to mRNA binding. Overall, the native human samples provide a near-complete molecular picture of the architecture and sophisticated interaction network of the 43S-bound eIF3 complex and the eIF2 ternary complex containing the initiator tRNA. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11439.map.gz | 140.7 MB | EMDB map data format | |
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Header (meta data) | emd-11439-v30.xml emd-11439.xml | 66 KB 66 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_11439_fsc.xml | 12.9 KB | Display | FSC data file |
Images | emd_11439.png | 58.1 KB | ||
Filedesc metadata | emd-11439.cif.gz | 14.5 KB | ||
Others | emd_11439_half_map_1.map.gz emd_11439_half_map_2.map.gz | 141.1 MB 140.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11439 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11439 | HTTPS FTP |
-Validation report
Summary document | emd_11439_validation.pdf.gz | 1012.5 KB | Display | EMDB validaton report |
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Full document | emd_11439_full_validation.pdf.gz | 1012.1 KB | Display | |
Data in XML | emd_11439_validation.xml.gz | 20.4 KB | Display | |
Data in CIF | emd_11439_validation.cif.gz | 26.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11439 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11439 | HTTPS FTP |
-Related structure data
Related structure data | 6zu9MC 6zceC 6zvjC 7a09C 7a1gC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_11439.map.gz / Format: CCP4 / Size: 178 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: 1.084 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: #2
File | emd_11439_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_11439_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : ABCE1-bound 48S initiation complex
+Supramolecule #1: ABCE1-bound 48S initiation complex
+Macromolecule #1: 18S ribosomal RNA
+Macromolecule #37: tRNA
+Macromolecule #42: mRNA
+Macromolecule #2: 40S ribosomal protein S0-A
+Macromolecule #3: 40S ribosomal protein S1-A
+Macromolecule #4: 40S ribosomal protein S2
+Macromolecule #5: 40S ribosomal protein S4-A
+Macromolecule #6: 40S ribosomal protein S6-A
+Macromolecule #7: 40S ribosomal protein S7-A
+Macromolecule #8: 40S ribosomal protein S8-A
+Macromolecule #9: 40S ribosomal protein S9-A
+Macromolecule #10: 40S ribosomal protein S11-A
+Macromolecule #11: 40S ribosomal protein S13
+Macromolecule #12: 40S ribosomal protein S14-A
+Macromolecule #13: 40S ribosomal protein S21-A
+Macromolecule #14: 40S ribosomal protein S22-A
+Macromolecule #15: 40S ribosomal protein S23-A
+Macromolecule #16: 40S ribosomal protein S24-A
+Macromolecule #17: 40S ribosomal protein S26-A
+Macromolecule #18: 40S ribosomal protein S27-A
+Macromolecule #19: 40S ribosomal protein S30-A
+Macromolecule #20: 40S ribosomal protein S15
+Macromolecule #21: 40S ribosomal protein S3
+Macromolecule #22: Rps5p
+Macromolecule #23: 40S ribosomal protein S10-A
+Macromolecule #24: 40S ribosomal protein S12
+Macromolecule #25: 40S ribosomal protein S16-A
+Macromolecule #26: 40S ribosomal protein S17-A
+Macromolecule #27: 40S ribosomal protein S18-A
+Macromolecule #28: 40S ribosomal protein S19-A
+Macromolecule #29: 40S ribosomal protein S20
+Macromolecule #30: 40S ribosomal protein S25-A
+Macromolecule #31: 40S ribosomal protein S29-A
+Macromolecule #32: Ubiquitin-40S ribosomal protein S31
+Macromolecule #33: Guanine nucleotide-binding protein subunit beta-like protein
+Macromolecule #34: 40S ribosomal protein S28-B
+Macromolecule #35: Eukaryotic translation initiation factor 3 subunit I
+Macromolecule #36: Eukaryotic translation initiation factor 3 subunit G
+Macromolecule #38: Eukaryotic translation initiation factor 5
+Macromolecule #39: Eukaryotic translation initiation factor 3 subunit A
+Macromolecule #40: Eukaryotic translation initiation factor 3 subunit B
+Macromolecule #41: Eukaryotic translation initiation factor 3 subunit C
+Macromolecule #43: Eukaryotic translation initiation factor 1A
+Macromolecule #44: Translation initiation factor RLI1
+Macromolecule #45: MAGNESIUM ION
+Macromolecule #46: ZINC ION
+Macromolecule #47: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #48: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #49: IRON/SULFUR CLUSTER
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 2.5 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |