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Yorodumi- PDB-7d5t: Cryo-EM structure of 90S preribosome with inactive Utp24 (state F1) -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7d5t | |||||||||
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| Title | Cryo-EM structure of 90S preribosome with inactive Utp24 (state F1) | |||||||||
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Keywords | RIBOSOME / ribosome assembly / 90S to pre-40S transition / cryo-EM / Dhr1 / Utp24 | |||||||||
| Function / homology | Function and homology informationregulation of ribosomal protein gene transcription by RNA polymerase II / box H/ACA snoRNA binding / RNA fragment catabolic process / CURI complex / UTP-C complex / rRNA 2'-O-methylation / Noc4p-Nop14p complex / endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / t-UTP complex / Pwp2p-containing subcomplex of 90S preribosome ...regulation of ribosomal protein gene transcription by RNA polymerase II / box H/ACA snoRNA binding / RNA fragment catabolic process / CURI complex / UTP-C complex / rRNA 2'-O-methylation / Noc4p-Nop14p complex / endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / t-UTP complex / Pwp2p-containing subcomplex of 90S preribosome / snoRNA guided rRNA 2'-O-methylation / Mpp10 complex / box C/D sno(s)RNA binding / rRNA modification / histone H2AQ104 methyltransferase activity / septum digestion after cytokinesis / regulation of rRNA processing / snRNA binding / RNA folding chaperone / box C/D sno(s)RNA 3'-end processing / rRNA methyltransferase activity / rDNA heterochromatin / endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / regulation of transcription by RNA polymerase I / endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / box C/D methylation guide snoRNP complex / U4/U6 snRNP / positive regulation of rRNA processing / tRNA export from nucleus / single-stranded telomeric DNA binding / rRNA primary transcript binding / sno(s)RNA-containing ribonucleoprotein complex / Negative regulators of DDX58/IFIH1 signaling / U4 snRNA binding / O-methyltransferase activity / SUMOylation of RNA binding proteins / 90S preribosome assembly / protein localization to nucleolus / mTORC1-mediated signalling / rRNA methylation / Protein hydroxylation / U4 snRNP / poly(U) RNA binding / U3 snoRNA binding / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / Ribosomal scanning and start codon recognition / snoRNA binding / precatalytic spliceosome / preribosome, small subunit precursor / Major pathway of rRNA processing in the nucleolus and cytosol / establishment of cell polarity / spliceosomal complex assembly / positive regulation of transcription by RNA polymerase I / SRP-dependent cotranslational protein targeting to membrane / nucleolar large rRNA transcription by RNA polymerase I / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Formation of a pool of free 40S subunits / L13a-mediated translational silencing of Ceruloplasmin expression / 90S preribosome / Ub-specific processing proteases / ribosomal subunit export from nucleus / RNA processing / regulation of translational fidelity / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / U4/U6 x U5 tri-snRNP complex / RNA endonuclease activity / Transferases; Transferring one-carbon groups; Methyltransferases / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / spliceosomal complex / small-subunit processome / translational initiation / enzyme activator activity / helicase activity / mRNA splicing, via spliceosome / maintenance of translational fidelity / rRNA processing / peroxisome / ribosome biogenesis / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cytoplasmic translation / RNA helicase activity / rRNA binding / structural constituent of ribosome / RNA helicase / ribosome / translation / GTPase activity / mRNA binding / GTP binding / nucleolus Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6 Å | |||||||||
Authors | Du, Y. / Zhang, J. / An, W. / Ye, K. | |||||||||
| Funding support | China, 2items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of 90S preribosome with inactive Utp24 (state F1) Authors: Ye, K. | |||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7d5t.cif.gz | 3.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7d5t.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7d5t.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7d5t_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 7d5t_full_validation.pdf.gz | 1.9 MB | Display | |
| Data in XML | 7d5t_validation.xml.gz | 439 KB | Display | |
| Data in CIF | 7d5t_validation.cif.gz | 711.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d5/7d5t ftp://data.pdbj.org/pub/pdb/validation_reports/d5/7d5t | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 30585MC ![]() 7d4iC ![]() 7d5sC ![]() 7d63C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 3 types, 3 molecules 3A5ASA
| #1: RNA chain | Mass: 106503.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: RNA chain | Mass: 225543.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: RNA chain | Mass: 583714.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-40S ribosomal protein ... , 16 types, 16 molecules SCSFSGSHSISJSKSMSOSPSRSXSYSZScSd
| #4: Protein | Mass: 28798.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P33442 |
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| #5: Protein | Mass: 29469.330 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX35 |
| #6: Protein | Mass: 25072.600 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P26783 |
| #7: Protein | Mass: 27054.486 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX37 |
| #8: Protein | Mass: 21658.209 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P26786 |
| #9: Protein | Mass: 22537.803 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX39 |
| #10: Protein | Mass: 22487.893 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: O13516 |
| #11: Protein | Mass: 17785.934 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX47 |
| #12: Protein | Mass: 17059.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P05756 |
| #13: Protein | Mass: 14562.655 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P06367 |
| #14: Protein | Mass: 15877.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX51 |
| #15: Protein | Mass: 14650.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q3E7Y3 |
| #16: Protein | Mass: 16073.896 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX29 |
| #17: Protein | Mass: 15362.848 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P0CX31 |
| #18: Protein | Mass: 8893.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P35997 |
| #19: Protein | Mass: 7605.847 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q3E7X9 |
-Protein , 13 types, 15 molecules 3B3C3G3HAGB15H5IRDRJRKRNRTRZX1
| #20: Protein | Mass: 34525.418 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c References: UniProt: P15646, Transferases; Transferring one-carbon groups; Methyltransferases #24: Protein | Mass: 13582.855 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P39990 #27: Protein | | Mass: 101341.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q02931 #28: Protein | | Mass: 101467.367 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P25635 #39: Protein | | Mass: 70364.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q12136 #40: Protein | | Mass: 56888.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P33750 #43: Protein | | Mass: 193411.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q05022 #46: Protein | | Mass: 135792.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q08965 #47: Protein | | Mass: 40220.559 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q08096 #48: Protein | | Mass: 94463.195 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q99207 #51: Protein | | Mass: 36356.477 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #52: Protein | | Mass: 145171.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q04217, RNA helicase #53: Protein | | Mass: 25549.350 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Nucleolar protein ... , 2 types, 2 molecules 3D3E
| #21: Protein | Mass: 56961.152 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q12460 |
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| #22: Protein | Mass: 57060.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q12499 |
-Ribosomal RNA-processing protein ... , 2 types, 2 molecules 3FRF
| #23: Protein | Mass: 65146.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q06506 |
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| #45: Protein | Mass: 34526.441 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P25368 |
-U3 small nucleolar RNA-associated protein ... , 13 types, 13 molecules A5AEB2B3B8BEB65C5D5ERERPRQ
| #25: Protein | Mass: 72079.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q04177 |
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| #26: Protein | Mass: 200298.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P42945 |
| #29: Protein | Mass: 106481.133 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q12220 |
| #30: Protein | Mass: 91132.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q05946 |
| #31: Protein | Mass: 66494.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P40362 |
| #32: Protein | Mass: 104927.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q06078 |
| #33: Protein | Mass: 52495.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q02354 |
| #34: Protein | Mass: 62418.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P40055 |
| #35: Protein | Mass: 29806.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P34247 |
| #36: Protein | Mass: 67042.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P47083 |
| #44: Protein | Mass: 140660.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P53254 |
| #49: Protein | Mass: 287915.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P35194 |
| #50: Protein | Mass: 103189.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q04500 |
-U3 small nucleolar ribonucleoprotein protein ... , 2 types, 2 molecules 5F5G
| #37: Protein | Mass: 21928.529 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P32899 |
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| #38: Protein | Mass: 33536.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P53941 |
-RRNA-processing protein ... , 2 types, 2 molecules 5J5K
| #41: Protein | Mass: 25689.240 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q12035 |
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| #42: Protein | Mass: 21649.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q05498 |
-Non-polymers , 4 types, 5 molecules 






| #54: Chemical | | #55: Chemical | ChemComp-GTP / | #56: Chemical | ChemComp-MG / | #57: Chemical | ChemComp-ADP / | |
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-Details
| Has ligand of interest | N |
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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 |
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Sample preparation
| Component | Name: 90S pre-ribosome (state F1) / Type: COMPLEX / Entity ID: #1-#53 / Source: NATURAL | |||||||||||||||
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| Molecular weight | Value: 5 MDa / Experimental value: NO | |||||||||||||||
| Source (natural) | Organism: ![]() | |||||||||||||||
| Buffer solution | pH: 7.4 | |||||||||||||||
| Buffer component |
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| Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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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 / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 10 / Num. of real images: 18538 |
| Image scans | Movie frames/image: 32 / Used frames/image: 1-32 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 913852 | ||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 62400 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 7D4I Accession code: 7D4I / Source name: PDB / Type: experimental model |
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