[English] 日本語
Yorodumi- PDB-6rxx: Cryo-EM structure of the 90S pre-ribosome (Kre33-Noc4) from Chaet... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6rxx | ||||||
---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of the 90S pre-ribosome (Kre33-Noc4) from Chaetomium thermophilum, state C, Poly-Ala | ||||||
Components |
| ||||||
Keywords | RIBOSOME / ribosome biogenesis / rRNA | ||||||
Function / homology | Function and homology information rRNA acetylation involved in maturation of SSU-rRNA / tRNA N-acetyltransferase activity / tRNA acetylation / Mpp10 complex / rRNA (pseudouridine) methyltransferase activity / intracellular organelle / box C/D methylation guide snoRNP complex / rRNA base methylation / rRNA primary transcript binding / sno(s)RNA-containing ribonucleoprotein complex ...rRNA acetylation involved in maturation of SSU-rRNA / tRNA N-acetyltransferase activity / tRNA acetylation / Mpp10 complex / rRNA (pseudouridine) methyltransferase activity / intracellular organelle / box C/D methylation guide snoRNP complex / rRNA base methylation / rRNA primary transcript binding / sno(s)RNA-containing ribonucleoprotein complex / U3 snoRNA binding / snoRNA binding / positive regulation of transcription by RNA polymerase I / 90S preribosome / catalytic activity / RNA processing / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / methyltransferase activity / small-subunit processome / spliceosomal complex / mRNA splicing, via spliceosome / rRNA processing / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / ribosome biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / methylation / rRNA binding / ribosome / protein ubiquitination / structural constituent of ribosome / translation / ribonucleoprotein complex / intracellular membrane-bounded organelle / nucleolus / GTP binding / RNA binding / ATP binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Chaetomium thermophilum (fungus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.1 Å | ||||||
Authors | Cheng, J. / Kellner, N. / Griesel, S. / Berninghausen, O. / Beckmann, R. / Hurt, E. | ||||||
Citation | Journal: Mol Cell / Year: 2019 Title: Thermophile 90S Pre-ribosome Structures Reveal the Reverse Order of Co-transcriptional 18S rRNA Subdomain Integration. Authors: Jingdong Cheng / Jochen Baßler / Paulina Fischer / Benjamin Lau / Nikola Kellner / Ruth Kunze / Sabine Griesel / Martina Kallas / Otto Berninghausen / Daniela Strauss / Roland Beckmann / Ed Hurt / Abstract: Eukaryotic ribosome biogenesis involves RNA folding and processing that depend on assembly factors and small nucleolar RNAs (snoRNAs). The 90S (SSU-processome) is the earliest pre-ribosome ...Eukaryotic ribosome biogenesis involves RNA folding and processing that depend on assembly factors and small nucleolar RNAs (snoRNAs). The 90S (SSU-processome) is the earliest pre-ribosome structurally analyzed, which was suggested to assemble stepwise along the growing pre-rRNA from 5' > 3', but this directionality may not be accurate. Here, by analyzing the structure of a series of 90S assembly intermediates from Chaetomium thermophilum, we discover a reverse order of 18S rRNA subdomain incorporation. Large parts of the 18S rRNA 3' and central domains assemble first into the 90S before the 5' domain is integrated. This final incorporation depends on a contact between a heterotrimer Enp2-Bfr2-Lcp5 recruited to the flexible 5' domain and Kre33, which reconstitutes the Kre33-Enp-Brf2-Lcp5 module on the compacted 90S. Keeping the 5' domain temporarily segregated from the 90S scaffold could provide extra time to complete the multifaceted 5' domain folding, which depends on a distinct set of snoRNAs and processing factors. | ||||||
History |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6rxx.cif.gz | 4.1 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6rxx.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6rxx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6rxx_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 6rxx_full_validation.pdf.gz | 1.6 MB | Display | |
Data in XML | 6rxx_validation.xml.gz | 446.7 KB | Display | |
Data in CIF | 6rxx_validation.cif.gz | 796.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rx/6rxx ftp://data.pdbj.org/pub/pdb/validation_reports/rx/6rxx | HTTPS FTP |
-Related structure data
Related structure data | 10054MC 6rxtC 6rxuC 6rxvC 6rxyC 6rxzC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
+Protein , 41 types, 46 molecules UAUCUFUGULUMUNURUUUXCJCMCNCOCPCQCqCUCVClCHCICRCSCWUTCZUBUDUJ...
-U3 small nucleolar RNA-associated protein ... , 2 types, 2 molecules UKUV
#5: Protein | Mass: 31379.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SF32 |
---|---|
#32: Protein | Mass: 131105.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S2E0 |
-Putative U3 small nucleolar ... , 2 types, 2 molecules CKCL
#13: Protein | Mass: 34216.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SE90 |
---|---|
#14: Protein | Mass: 86082.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S9I7 |
-40S ribosomal protein ... , 16 types, 16 molecules CaCcCeCgChCiCjCmCnCpCbCdCfCkCoCr
#19: Protein | Mass: 29245.158 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S7T8 |
---|---|
#20: Protein | Mass: 23679.225 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S1Z0 |
#21: Protein | Mass: 23084.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S8C4 |
#22: Protein | Mass: 22029.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S0Z4 |
#23: Protein | Mass: 16912.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0RZM9 |
#24: Protein | Mass: 16071.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SFL1 |
#25: Protein | Mass: 15962.771 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SBR7 |
#26: Protein | Mass: 14905.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SHI0 |
#27: Protein | Mass: 15934.653 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0RY17 |
#28: Protein | Mass: 7741.980 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S9M9 |
#38: Protein | Mass: 29800.764 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0S1A6 |
#39: Protein | Mass: 27490.139 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0RY43 |
#40: Protein | Mass: 23102.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0RY45 |
#41: Protein | Mass: 18698.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SF00 |
#42: Protein | Mass: 15535.286 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: P0CU28 |
#63: Protein | Mass: 17151.332 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) / References: UniProt: G0SFK8 |
-RNA chain , 2 types, 2 molecules C1C2
#31: RNA chain | Mass: 599293.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) |
---|---|
#62: RNA chain | Mass: 74578.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chaetomium thermophilum (fungus) |
-Non-polymers , 1 types, 2 molecules
#64: Chemical |
---|
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: 90S pre-ribosome, state C / Type: RIBOSOME / Entity ID: #1-#63 / Source: NATURAL |
---|---|
Source (natural) | Organism: Chaetomium thermophilum (fungus) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 28 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
-Processing
EM software |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||
3D reconstruction | Resolution: 7.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 9041 / Symmetry type: POINT |