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Yorodumi- EMDB-10519: Structure of an archaeal ABCE1-bound ribosomal post-splitting complex -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-10519 | |||||||||
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Title | Structure of an archaeal ABCE1-bound ribosomal post-splitting complex | |||||||||
Map data | composite map of post-processed maps | |||||||||
Sample |
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Keywords | ABC Proteins / Ribosome Recycling / Translation / RIBOSOME | |||||||||
Function / homology | Function and homology information ribonuclease P activity / tRNA 5'-leader removal / ribosomal small subunit binding / translational termination / translational initiation / ribosome biogenesis / small ribosomal subunit / tRNA binding / oxidoreductase activity / rRNA binding ...ribonuclease P activity / tRNA 5'-leader removal / ribosomal small subunit binding / translational termination / translational initiation / ribosome biogenesis / small ribosomal subunit / tRNA binding / oxidoreductase activity / rRNA binding / ribosome / structural constituent of ribosome / iron ion binding / translation / ribonucleoprotein complex / ATP hydrolysis activity / zinc ion binding / ATP binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Thermococcus celer Vu 13 = JCM 8558 (archaea) / Saccharolobus solfataricus (archaea) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Kratzat H / Becker T | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: EMBO J / Year: 2020 Title: Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex. Authors: Elina Nürenberg-Goloub / Hanna Kratzat / Holger Heinemann / André Heuer / Peter Kötter / Otto Berninghausen / Thomas Becker / Robert Tampé / Roland Beckmann / Abstract: Ribosome recycling by the twin-ATPase ABCE1 is a key regulatory process in mRNA translation and surveillance and in ribosome-associated protein quality control in Eukarya and Archaea. Here, we ...Ribosome recycling by the twin-ATPase ABCE1 is a key regulatory process in mRNA translation and surveillance and in ribosome-associated protein quality control in Eukarya and Archaea. Here, we captured the archaeal 30S ribosome post-splitting complex at 2.8 Å resolution by cryo-electron microscopy. The structure reveals the dynamic behavior of structural motifs unique to ABCE1, which ultimately leads to ribosome splitting. More specifically, we provide molecular details on how conformational rearrangements of the iron-sulfur cluster domain and hinge regions of ABCE1 are linked to closure of its nucleotide-binding sites. The combination of mutational and functional analyses uncovers an intricate allosteric network between the ribosome, regulatory domains of ABCE1, and its two structurally and functionally asymmetric ATP-binding sites. Based on these data, we propose a refined model of how signals from the ribosome are integrated into the ATPase cycle of ABCE1 to orchestrate ribosome recycling. | |||||||||
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_10519.map.gz | 22 MB | EMDB map data format | |
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Header (meta data) | emd-10519-v30.xml emd-10519.xml | 52.3 KB 52.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_10519_fsc.xml | 12.7 KB | Display | FSC data file |
Images | emd_10519.png | 56.9 KB | ||
Filedesc metadata | emd-10519.cif.gz | 10.5 KB | ||
Others | emd_10519_additional_1.map.gz emd_10519_additional_2.map.gz emd_10519_additional_3.map.gz | 5.2 MB 19.1 MB 8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-10519 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-10519 | HTTPS FTP |
-Validation report
Summary document | emd_10519_validation.pdf.gz | 259.2 KB | Display | EMDB validaton report |
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Full document | emd_10519_full_validation.pdf.gz | 258.3 KB | Display | |
Data in XML | emd_10519_validation.xml.gz | 13.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10519 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10519 | HTTPS FTP |
-Related structure data
Related structure data | 6tmfMC 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_10519.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | composite map of post-processed maps | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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
-Additional map: post-processed map of ABCE1 after focused refinement
File | emd_10519_additional_1.map | ||||||||||||
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Annotation | post-processed map of ABCE1 after focused refinement | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: post-processed map of the whole complex
File | emd_10519_additional_2.map | ||||||||||||
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Annotation | post-processed map of the whole complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: post-processed map of the 30S head after focused refinement
File | emd_10519_additional_3.map | ||||||||||||
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Annotation | post-processed map of the 30S head after focused refinement | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 30S ABCE1 post-splitting complex
+Supramolecule #1: 30S ABCE1 post-splitting complex
+Supramolecule #2: 30S small ribosomal subunit
+Supramolecule #3: ABCE1
+Macromolecule #1: 16S ribosomal RNA
+Macromolecule #2: 30S ribosomal protein S2
+Macromolecule #3: 30S ribosomal protein S3
+Macromolecule #4: 30S ribosomal protein S3Ae
+Macromolecule #5: 30S ribosomal protein S4
+Macromolecule #6: 30S ribosomal protein S4e
+Macromolecule #7: 30S ribosomal protein S5
+Macromolecule #8: 30S ribosomal protein S6e
+Macromolecule #9: 30S ribosomal protein S7
+Macromolecule #10: 30S ribosomal protein S8
+Macromolecule #11: 30S ribosomal protein S8e
+Macromolecule #12: 30S ribosomal protein S9
+Macromolecule #13: 30S ribosomal protein S10
+Macromolecule #14: 30S ribosomal protein S11
+Macromolecule #15: 30S ribosomal protein S12
+Macromolecule #16: 30S ribosomal protein S13
+Macromolecule #17: 30S ribosomal protein S14 type Z
+Macromolecule #18: 30S ribosomal protein S15
+Macromolecule #19: 30S ribosomal protein S17
+Macromolecule #20: 30S ribosomal protein S17e
+Macromolecule #21: 30S ribosomal protein S19P
+Macromolecule #22: 30S ribosomal protein S19e
+Macromolecule #23: RNA-binding protein
+Macromolecule #24: 30S ribosomal protein S24e
+Macromolecule #25: 30S ribosomal protein S27e
+Macromolecule #26: 30S ribosomal protein S27ae
+Macromolecule #27: 30S ribosomal protein S28e
+Macromolecule #28: 50S ribosomal protein L7Ae
+Macromolecule #29: LSU ribosomal protein L41E
+Macromolecule #30: ATPase
+Macromolecule #31: MAGNESIUM ION
+Macromolecule #32: ZINC ION
+Macromolecule #33: IRON/SULFUR CLUSTER
+Macromolecule #34: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
-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: 25.0 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 |