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Yorodumi- EMDB-17956: Chaetomium thermophilum pre-60S State 1 - pre-5S rotation (Arx1/N... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17956 | ||||||||||||
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Title | Chaetomium thermophilum pre-60S State 1 - pre-5S rotation (Arx1/Nog2 state) - Composite structure | ||||||||||||
Map data | Chaetomium thermophilum pre-60S State 1 - pre-5S rotation (Arx1/Nog2 state) - composite structure | ||||||||||||
Sample |
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Keywords | biogenesis / pre-60S / 5S RNP / RIBOSOME | ||||||||||||
Function / homology | Function and homology information dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit binding / protein glycosylation / preribosome, large subunit precursor / protein-RNA complex assembly / ribonucleoprotein complex binding / ribosomal subunit export from nucleus / maturation of LSU-rRNA ...dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit binding / protein glycosylation / preribosome, large subunit precursor / protein-RNA complex assembly / ribonucleoprotein complex binding / ribosomal subunit export from nucleus / maturation of LSU-rRNA / translation initiation factor activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / cytosolic ribosome assembly / rRNA processing / large ribosomal subunit / ribosome biogenesis / 5S rRNA binding / large ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / nucleic acid binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / GTP binding / nucleolus / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Thermochaetoides thermophila DSM 1495 (fungus) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.12 Å | ||||||||||||
Authors | Thoms M / Cheng J / Denk T / Berninghausen O / Beckmann R | ||||||||||||
Funding support | European Union, Germany, 3 items
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Citation | Journal: EMBO Rep / Year: 2023 Title: Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation. Authors: Matthias Thoms / Benjamin Lau / Jingdong Cheng / Lisa Fromm / Timo Denk / Nikola Kellner / Dirk Flemming / Paulina Fischer / Laurent Falquet / Otto Berninghausen / Roland Beckmann / Ed Hurt / Abstract: The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from ...The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from Chaetomium thermophilum, which consists of two sub-modules, the sphere-like Rix1-Ipi3-Ipi1 and the butterfly-like Las1-Grc3 complex, connected by a flexible linker. The Rix1 complex of the rixosome utilizes Sda1 as landing platform on nucleoplasmic pre-60S particles to wedge between the 5S rRNA tip and L1-stalk, thereby facilitating the 180° rotation of the immature 5S RNP towards its mature conformation. Upon rixosome positioning, the other sub-module with Las1 endonuclease and Grc3 polynucleotide-kinase can reach a strategic position at the pre-60S foot to cleave and 5' phosphorylate the nearby ITS2 pre-rRNA. Finally, inward movement of the L1 stalk permits the flexible Nop53 N-terminus with its AIM motif to become positioned at the base of the L1-stalk to facilitate Mtr4 helicase-exosome participation for completing ITS2 removal. Thus, the rixosome structure elucidates the coordination of two central ribosome biogenesis events, but its role in gene silencing may adapt similar strategies. | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17956.map.gz | 16.7 MB | EMDB map data format | |
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Header (meta data) | emd-17956-v30.xml emd-17956.xml | 90.9 KB 90.9 KB | Display Display | EMDB header |
Images | emd_17956.png | 94.2 KB | ||
Filedesc metadata | emd-17956.cif.gz | 20.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17956 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17956 | HTTPS FTP |
-Validation report
Summary document | emd_17956_validation.pdf.gz | 405.3 KB | Display | EMDB validaton report |
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Full document | emd_17956_full_validation.pdf.gz | 404.9 KB | Display | |
Data in XML | emd_17956_validation.xml.gz | 7.7 KB | Display | |
Data in CIF | emd_17956_validation.cif.gz | 8.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17956 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17956 | HTTPS FTP |
-Related structure data
Related structure data | 8pv7MC 8ptwC 8puwC 8pv1C 8pv2C 8pv3C 8pv4C 8pv5C 8pv6C 8pv8C 8pvkC 8pvlC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_17956.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Chaetomium thermophilum pre-60S State 1 - pre-5S rotation (Arx1/Nog2 state) - composite structure | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.045 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
+Entire : Chaetomium thermophilum pre-60S State 1 - pre-5S rotation (Arx1/N...
+Supramolecule #1: Chaetomium thermophilum pre-60S State 1 - pre-5S rotation (Arx1/N...
+Supramolecule #2: Ribosome
+Supramolecule #3: Ribosome assembly protein 4
+Macromolecule #1: 26S rRNA
+Macromolecule #2: 5.8S rRNA
+Macromolecule #3: ITS2
+Macromolecule #4: 5S rRNA
+Macromolecule #5: Utp30
+Macromolecule #6: Large ribosomal subunit protein uL10
+Macromolecule #7: Nucleolar GTP-binding protein 1
+Macromolecule #8: Putative RNA-binding protein
+Macromolecule #9: Pescadillo homolog
+Macromolecule #10: Ribosome biogenesis protein NSA2 homolog
+Macromolecule #11: Putative GTP binding protein
+Macromolecule #12: 60S ribosomal protein l7-like protein
+Macromolecule #13: Eukaryotic translation initiation factor 6
+Macromolecule #14: DUF2423 domain-containing protein
+Macromolecule #15: Ribosome biogenesis protein RLP24
+Macromolecule #16: Putative 60S ribosomal protein
+Macromolecule #17: Zinc finger domain-containing protein
+Macromolecule #18: Nucleolar GTP-binding protein 2
+Macromolecule #19: Ribosome biogenesis protein NOP53
+Macromolecule #20: Ribosome production factor 2 homolog
+Macromolecule #21: Ribosome biogenesis regulatory protein
+Macromolecule #22: Ribosome assembly protein 4
+Macromolecule #23: rRNA-processing protein
+Macromolecule #24: 60S ribosomal protein L2-like protein
+Macromolecule #25: 60S ribosomal protein L3-like protein
+Macromolecule #26: 60S ribosomal protein L4-like protein
+Macromolecule #27: 60S ribosomal protein l5-like protein
+Macromolecule #28: 60S ribosomal protein L6
+Macromolecule #29: 60S ribosomal protein L8
+Macromolecule #30: 60S ribosomal protein l9-like protein
+Macromolecule #31: Putative ribosomal protein
+Macromolecule #32: 60S ribosomal protein L12-like protein
+Macromolecule #33: 60S ribosomal protein L13
+Macromolecule #34: 60S ribosomal protein L14-like protein
+Macromolecule #35: Ribosomal protein L15
+Macromolecule #36: 60S ribosomal protein L16-like protein
+Macromolecule #37: 60S ribosomal protein l17-like protein
+Macromolecule #38: Ribosomal protein L18-like protein
+Macromolecule #39: Ribosomal protein L19
+Macromolecule #40: 60S ribosomal protein L20
+Macromolecule #41: 60S ribosomal protein l21-like protein
+Macromolecule #42: 60S ribosomal protein L22-like protein
+Macromolecule #43: 60S ribosomal protein l23-like protein
+Macromolecule #44: 60S ribosomal protein L25-like protein
+Macromolecule #45: 60S ribosomal protein L26-like protein
+Macromolecule #46: 60S ribosomal protein L27
+Macromolecule #47: 60S ribosomal protein L28-like protein
+Macromolecule #48: 60S ribosomal protein l30-like protein
+Macromolecule #49: Putative 60S ribosomal protein
+Macromolecule #50: 60S ribosomal protein L32-like protein
+Macromolecule #51: 60S ribosomal protein l33-like protein
+Macromolecule #52: Ribosomal protein l34-like protein
+Macromolecule #53: dolichyl-diphosphooligosaccharide--protein glycotransferase
+Macromolecule #54: 60S ribosomal protein L36
+Macromolecule #55: Ribosomal protein L37
+Macromolecule #56: 60S ribosomal protein L38-like protein
+Macromolecule #57: Ribosomal protein eL39
+Macromolecule #58: 60S ribosomal protein L43-like protein
+Macromolecule #59: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #60: MAGNESIUM ION
+Macromolecule #61: ZINC ION
+Macromolecule #62: water
-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: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 45.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / 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 |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.12 Å / Resolution method: FSC 0.143 CUT-OFF Details: Note: Values given relate to the consensus reconstruction Number images used: 745895 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |