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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Rea1 delta AAA2H2alpha ATPgS structure | |||||||||
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Keywords | AAA+ protein / ribosome maturation / TRANSLOCASE | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 7.1 Å | |||||||||
Authors | Busselez J / Schmidt H | |||||||||
| Funding support | France, 1 items
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Citation | Journal: Nat Commun / Year: 2024Title: Remodelling of Rea1 linker domain drives the removal of assembly factors from pre-ribosomal particles. Authors: Johan Busselez / Geraldine Koenig / Carine Dominique / Torben Klos / Deepika Velayudhan / Piotr Sosnowski / Nils Marechal / Corinne Crucifix / Hugo Gizardin-Fredon / Sarah Cianferani / ...Authors: Johan Busselez / Geraldine Koenig / Carine Dominique / Torben Klos / Deepika Velayudhan / Piotr Sosnowski / Nils Marechal / Corinne Crucifix / Hugo Gizardin-Fredon / Sarah Cianferani / Benjamin Albert / Yves Henry / Anthony K Henras / Helgo Schmidt / ![]() Abstract: The ribosome maturation factor Rea1 (or Midasin) catalyses the removal of assembly factors from large ribosomal subunit precursors and promotes their export from the nucleus to the cytosol. Rea1 ...The ribosome maturation factor Rea1 (or Midasin) catalyses the removal of assembly factors from large ribosomal subunit precursors and promotes their export from the nucleus to the cytosol. Rea1 consists of nearly 5000 amino-acid residues and belongs to the AAA+ protein family. It consists of a ring of six AAA+ domains from which the ≈1700 amino-acid residue linker emerges that is subdivided into stem, middle and top domains. A flexible and unstructured D/E rich region connects the linker top to a MIDAS (metal ion dependent adhesion site) domain, which is able to bind the assembly factor substrates. Despite its key importance for ribosome maturation, the mechanism driving assembly factor removal by Rea1 is still poorly understood. Here we demonstrate that the Rea1 linker is essential for assembly factor removal. It rotates and swings towards the AAA+ ring following a complex remodelling scheme involving nucleotide independent as well as nucleotide dependent steps. ATP-hydrolysis is required to engage the linker with the AAA+ ring and ultimately with the AAA+ ring docked MIDAS domain. The interaction between the linker top and the MIDAS domain allows direct force transmission for assembly factor removal. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_50815.map.gz | 745.3 KB | EMDB map data format | |
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| Header (meta data) | emd-50815-v30.xml emd-50815.xml | 12.6 KB 12.6 KB | Display Display | EMDB header |
| Images | emd_50815.png | 82 KB | ||
| Filedesc metadata | emd-50815.cif.gz | 4 KB | ||
| Others | emd_50815_half_map_1.map.gz emd_50815_half_map_2.map.gz | 6 MB 6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-50815 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-50815 | HTTPS FTP |
-Validation report
| Summary document | emd_50815_validation.pdf.gz | 559.1 KB | Display | EMDB validaton report |
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| Full document | emd_50815_full_validation.pdf.gz | 558.7 KB | Display | |
| Data in XML | emd_50815_validation.xml.gz | 8.3 KB | Display | |
| Data in CIF | emd_50815_validation.cif.gz | 9.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50815 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50815 | 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_50815.map.gz / Format: CCP4 / Size: 8 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: 3.448 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_50815_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_50815_half_map_2.map | ||||||||||||
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Sample components
-Entire : Rea1 monomer
| Entire | Name: Rea1 monomer |
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| Components |
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-Supramolecule #1: Rea1 monomer
| Supramolecule | Name: Rea1 monomer / type: organelle_or_cellular_component / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 500 KDa |
-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 | 1 mg/mL |
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| Buffer | pH: 7.5 |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK II |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 IS (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: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 7.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 230000 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
-Atomic model buiding 1
| Refinement | Protocol: RIGID BODY FIT |
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Keywords
Authors
France, 1 items
Citation



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FIELD EMISSION GUN

