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Yorodumi- PDB-5oql: Cryo-EM structure of the 90S pre-ribosome from Chaetomium thermophilum -
+Open data
-Basic information
Entry | Database: PDB / ID: 5oql | ||||||
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Title | Cryo-EM structure of the 90S pre-ribosome from Chaetomium thermophilum | ||||||
Components |
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Keywords | RIBOSOME / Ribosome biogenesis | ||||||
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 / box C/D methylation guide snoRNP complex / rRNA base methylation / rRNA primary transcript binding / sno(s)RNA-containing ribonucleoprotein complex / U3 snoRNA binding ...rRNA acetylation involved in maturation of SSU-rRNA / tRNA N-acetyltransferase activity / tRNA acetylation / Mpp10 complex / rRNA (pseudouridine) methyltransferase activity / 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 nuclease 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 / ribonucleoprotein complex / translation / GTP binding / nucleolus / RNA binding / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Chaetomium thermophilum (fungus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||
Authors | Cheng, J. / Kellner, N. / Berninghausen, O. / Hurt, E. / Beckmann, R. | ||||||
Citation | Journal: Nat Struct Mol Biol / Year: 2017 Title: 3.2-Å-resolution structure of the 90S preribosome before A1 pre-rRNA cleavage. Authors: Jingdong Cheng / Nikola Kellner / Otto Berninghausen / Ed Hurt / Roland Beckmann / Abstract: The 40S small ribosomal subunit is cotranscriptionally assembled in the nucleolus as part of a large chaperone complex called the 90S preribosome or small-subunit processome. Here, we present the 3.2- ...The 40S small ribosomal subunit is cotranscriptionally assembled in the nucleolus as part of a large chaperone complex called the 90S preribosome or small-subunit processome. Here, we present the 3.2-Å-resolution structure of the Chaetomium thermophilum 90S preribosome, which allowed us to build atomic structures for 34 assembly factors, including the Mpp10 complex, Bms1, Utp14 and Utp18, and the complete U3 small nucleolar ribonucleoprotein. Moreover, we visualized the U3 RNA heteroduplexes with a 5' external transcribed spacer (5' ETS) and pre-18S RNA, and their stabilization by 90S factors. Overall, the structure explains how a highly intertwined network of assembly factors and pre-rRNA guide the sequential, independent folding of the individual pre-40S domains while the RNA regions forming the 40S active sites are kept immature. Finally, by identifying the unprocessed A1 cleavage site and the nearby Utp24 endonuclease, we suggest a proofreading model for regulated 5'-ETS separation and 90S-pre-40S transition. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
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PDBx/mmCIF format | 5oql.cif.gz | 3.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5oql.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 5oql.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5oql_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 5oql_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 5oql_validation.xml.gz | 328.7 KB | Display | |
Data in CIF | 5oql_validation.cif.gz | 552.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oq/5oql ftp://data.pdbj.org/pub/pdb/validation_reports/oq/5oql | HTTPS FTP |
-Related structure data
Related structure data | 3847MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
+Protein , 32 types, 36 molecules ABCDEFGHIJKLMNOPQRSTUVWXYZadef...
-Putative U3 small nucleolar ... , 2 types, 2 molecules bc
#26: Protein | Mass: 34216.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0SE90 |
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#27: Protein | Mass: 86082.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S9I7 |
-40S ribosomal protein ... , 15 types, 15 molecules lmnopqrstuvwxyz
#34: Protein | Mass: 29245.158 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S7T8 |
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#35: Protein | Mass: 29800.764 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S1A6 |
#36: Protein | Mass: 23679.225 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S1Z0 |
#37: Protein | Mass: 27490.139 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0RY43 |
#38: Protein | Mass: 23084.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S8C4 |
#39: Protein | Mass: 23102.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0RY45 |
#40: Protein | Mass: 22029.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S0Z4 |
#41: Protein | Mass: 16912.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0RZM9 |
#42: Protein | Mass: 16071.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0SFL1 |
#43: Protein | Mass: 15962.771 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0SBR7 |
#44: Protein | Mass: 18698.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0SF00 |
#45: Protein | Mass: 14905.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0SHI0 |
#46: Protein | Mass: 15934.653 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0RY17 |
#47: Protein | Mass: 15535.286 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: P0CU28 |
#48: Protein | Mass: 7741.980 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) References: UniProt: G0S9M9 |
-RNA chain , 2 types, 2 molecules 12
#50: RNA chain | Mass: 827801.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) |
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#51: RNA chain | Mass: 87992.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) |
-Non-polymers , 1 types, 1 molecules
#52: Chemical | ChemComp-ZN / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: The 90S Pre-ribosomne / Type: COMPLEX / Entity ID: #1-#51 / Source: NATURAL |
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Source (natural) | Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (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 |
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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: 2.4 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.11.1_2575: / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 231121 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL | ||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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