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Yorodumi- EMDB-17957: Chaetomium thermophilum pre-60S State 4 - post-5S rotation with R... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17957 | |||||||||
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Title | Chaetomium thermophilum pre-60S State 4 - post-5S rotation with Rix1 complex without Foot - composite structure | |||||||||
Map data | Chaetomium thermophilum pre-60S State 4 - post-5S rotation with Rix1 complex without Foot - composite structure | |||||||||
Sample |
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Keywords | biogenesis / pre-60S / 5S RNP / RIBOSOME | |||||||||
Function / homology | Function and homology information rixosome complex / dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / ribosomal large subunit binding / protein glycosylation / ribosomal large subunit export from nucleus / 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) ...rixosome complex / dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / ribosomal large subunit binding / protein glycosylation / ribosomal large subunit export from nucleus / 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 / protein transport / 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 / membrane / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Thermochaetoides thermophila DSM 1495 (fungus) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.91 Å | |||||||||
Authors | Thoms M / Cheng J / Denk T / Berninghausen O / Beckmann R | |||||||||
Funding support | European Union, 1 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_17957.map.gz | 17.6 MB | EMDB map data format | |
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Header (meta data) | emd-17957-v30.xml emd-17957.xml | 89.6 KB 89.6 KB | Display Display | EMDB header |
Images | emd_17957.png | 158.3 KB | ||
Filedesc metadata | emd-17957.cif.gz | 20.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17957 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17957 | HTTPS FTP |
-Validation report
Summary document | emd_17957_validation.pdf.gz | 417.9 KB | Display | EMDB validaton report |
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Full document | emd_17957_full_validation.pdf.gz | 417.5 KB | Display | |
Data in XML | emd_17957_validation.xml.gz | 7.9 KB | Display | |
Data in CIF | emd_17957_validation.cif.gz | 9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17957 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17957 | HTTPS FTP |
-Related structure data
Related structure data | 8pv8MC 8ptwC 8puwC 8pv1C 8pv2C 8pv3C 8pv4C 8pv5C 8pv6C 8pv7C 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_17957.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 4 - post-5S rotation with Rix1 complex without Foot - 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 2 - pre-5S rotation with Ri...
+Supramolecule #1: Chaetomium thermophilum pre-60S State 2 - pre-5S rotation with Ri...
+Supramolecule #2: Ribosome
+Supramolecule #3: Ribosome assembly protein 4
+Macromolecule #1: 26S rRNA
+Macromolecule #2: 5.8S rRNA
+Macromolecule #54: 5S rRNA
+Macromolecule #3: Large ribosomal subunit protein uL10
+Macromolecule #4: Nucleolar GTP-binding protein 1
+Macromolecule #5: Ribosome biogenesis protein NSA2 homolog
+Macromolecule #6: Putative GTP binding protein
+Macromolecule #7: Eukaryotic translation initiation factor 6
+Macromolecule #8: DUF2423 domain-containing protein
+Macromolecule #9: Ribosome biogenesis protein RLP24
+Macromolecule #10: Zinc finger domain-containing protein
+Macromolecule #11: Nucleolar GTP-binding protein 2
+Macromolecule #12: rRNA-processing protein
+Macromolecule #13: 60S ribosomal protein L2-like protein
+Macromolecule #14: 60S ribosomal protein L3-like protein
+Macromolecule #15: 60S ribosomal protein L4-like protein
+Macromolecule #16: 60S ribosomal protein L6
+Macromolecule #17: 60S ribosomal protein l7-like protein
+Macromolecule #18: 60S ribosomal protein L8
+Macromolecule #19: 60S ribosomal protein l9-like protein
+Macromolecule #20: 60S ribosomal protein L12-like protein
+Macromolecule #21: 60S ribosomal protein L13
+Macromolecule #22: 60S ribosomal protein L14-like protein
+Macromolecule #23: Ribosomal protein L15
+Macromolecule #24: 60S ribosomal protein L16-like protein
+Macromolecule #25: 60S ribosomal protein l17-like protein
+Macromolecule #26: Ribosomal protein L18-like protein
+Macromolecule #27: Ribosomal protein L19
+Macromolecule #28: 60S ribosomal protein L20
+Macromolecule #29: 60S ribosomal protein L22-like protein
+Macromolecule #30: 60S ribosomal protein l23-like protein
+Macromolecule #31: 60S ribosomal protein L25-like protein
+Macromolecule #32: 60S ribosomal protein L26-like protein
+Macromolecule #33: 60S ribosomal protein L27
+Macromolecule #34: 60S ribosomal protein L28-like protein
+Macromolecule #35: 60S ribosomal protein l30-like protein
+Macromolecule #36: Putative 60S ribosomal protein
+Macromolecule #37: 60S ribosomal protein L32-like protein
+Macromolecule #38: 60S ribosomal protein l33-like protein
+Macromolecule #39: Ribosomal protein l34-like protein
+Macromolecule #40: dolichyl-diphosphooligosaccharide--protein glycotransferase
+Macromolecule #41: 60S ribosomal protein L36
+Macromolecule #42: Ribosomal protein L37
+Macromolecule #43: 60S ribosomal protein L38-like protein
+Macromolecule #44: Ribosomal protein eL39
+Macromolecule #45: 60S ribosomal protein L43-like protein
+Macromolecule #46: Pre-rRNA-processing protein IPI3
+Macromolecule #47: Pre-rRNA-processing protein RIX1
+Macromolecule #48: Pre-rRNA-processing protein IPI1
+Macromolecule #49: Protein SDA1
+Macromolecule #50: Ribosomal protein
+Macromolecule #51: Ribosome assembly protein 4
+Macromolecule #52: Putative ribosomal protein
+Macromolecule #53: 60S ribosomal protein l5-like protein
+Macromolecule #55: Putative 60S ribosomal protein
+Macromolecule #56: 60S ribosomal protein l21-like protein
+Macromolecule #57: 60S ribosomal protein L29
+Macromolecule #58: 60S ribosomal protein L41-A
+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: 46.0 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: 0.4 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: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF Details: Note: This is a composite structure. Values given for consensus refinement. Number images used: 21061 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |