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Yorodumi- PDB-9xa9: Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Ch... -
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Basic information
| Entry | Database: PDB / ID: 9xa9 | ||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Tsr1-1 | ||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / 90S / pre-40S ribosome / Rrp12 / Enp1 / ribosome biogenesis | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology information90S preribosome / cytosolic ribosome / methyltransferase activity / small-subunit processome / rRNA processing / ribosomal small subunit assembly / ribosome biogenesis / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding ...90S preribosome / cytosolic ribosome / methyltransferase activity / small-subunit processome / rRNA processing / ribosomal small subunit assembly / ribosome biogenesis / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / methylation / cytoplasmic translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / nucleolus / RNA binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Thermochaetoides thermophila (fungus) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||||||||||||||
Authors | Lau, B. / Li, Y. / Zhu, J. / Fischer, P. / Hong, X. / Yuan, R. / Beckmann, R. / Hurt, E. / Cheng, J. | ||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: Cell Rep / Year: 2026Title: Nucleoplasmic checkpoint of the 40S ribosomal decoding center maturation. Authors: Benjamin Lau / Yi Li / Jingyi Zhu / Xianwen Ye / Paulina Fischer / Xiaying Hong / Rui Yuan / Roland Beckmann / Ed Hurt / Jingdong Cheng / ![]() Abstract: The decoding center (DC) is a key ribosomal structure for accurate translation, assembled in a multi-step process that starts on nucleolar pre-ribosomes and ends in the cytoplasm. While late ...The decoding center (DC) is a key ribosomal structure for accurate translation, assembled in a multi-step process that starts on nucleolar pre-ribosomes and ends in the cytoplasm. While late cytoplasmic steps and their checkpoint mechanisms are well characterized, the regulation of early nucleoplasmic DC assembly is unclear. Here, we show that the essential assembly factor Rrp12 plays a central coordinating role. Using Chaetomium thermophilum and cryo-electron microscopy analyses of fifteen pre-40S intermediates, we demonstrate that Rrp12 C terminus truncation: (1) inhibits release of the Utp14-Dhr1 pair, (2) displaces Tsr1, (3) promotes premature stabilization of h28, and (4) prevents h44 formation. These defects impair final 18S rRNA processing and prematurely activate the quality control kinase Rio1. Our results reveal a nucleoplasmic checkpoint during DC formation and establish Rrp12 as a critical regulator ensuring accurate assembly and orderly ribosome maturation. | ||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9xa9.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9xa9.ent.gz | 871 KB | Display | PDB format |
| PDBx/mmJSON format | 9xa9.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xa/9xa9 ftp://data.pdbj.org/pub/pdb/validation_reports/xa/9xa9 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 66679MC ![]() 9xa7C ![]() 9xa8C ![]() 9xaaC ![]() 9xabC ![]() 9xacC ![]() 9xadC ![]() 9xaeC ![]() 9xafC ![]() 9xagC ![]() 9xahC ![]() 9xaiC ![]() 9xajC ![]() 9xakC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Small ribosomal subunit protein ... , 4 types, 4 molecules DEFb
| #1: Protein | Mass: 31158.996 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RYF9 |
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| #2: Protein | Mass: 29245.158 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S7T8 |
| #3: Protein | Mass: 28556.115 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SAV4 |
| #16: Protein | Mass: 15535.286 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: P0CU28 |
-40S ribosomal protein ... , 13 types, 13 molecules HJKLMOQRUYZah
| #4: Protein | Mass: 29800.764 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S1A6 |
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| #5: Protein | Mass: 27490.139 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RY43 |
| #6: Protein | Mass: 23084.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S8C4 |
| #7: Protein | Mass: 23102.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RY45 |
| #8: Protein | Mass: 22029.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S0Z4 |
| #9: Protein | Mass: 18698.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SF00 |
| #10: Protein | Mass: 16912.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RZM9 |
| #11: Protein | Mass: 16071.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SFL1 |
| #12: Protein | Mass: 16720.240 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S871 |
| #13: Protein | Mass: 10961.475 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SI21 |
| #14: Protein | Mass: 14905.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SHI0 |
| #15: Protein | Mass: 15934.653 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RY17 |
| #18: Protein | Mass: 6917.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) |
-Protein , 2 types, 2 molecules e3
| #17: Protein | Mass: 8923.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S1S4 |
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| #20: Protein | Mass: 28715.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S3T2 |
-RNA chain , 1 types, 1 molecules A
| #19: RNA chain | Mass: 578795.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) |
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-Non-polymers , 3 types, 7 molecules 




| #21: Chemical | | #22: Chemical | ChemComp-ZN / | #23: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: pre-40S ribosome, state Tsr1-1 / Type: RIBOSOME / Entity ID: #1-#20 / Source: NATURAL |
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| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Details: Relion / Type: NONE | |||||||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 12066 / Symmetry type: POINT | |||||||||||||||||||||
| Atomic model building | PDB-ID: 6G18 Accession code: 6G18 / Source name: PDB / Type: experimental model |
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Thermochaetoides thermophila (fungus)
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FIELD EMISSION GUN
