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Open data
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Basic information
| Entry | Database: PDB / ID: 9qjc | ||||||||||||||||||||||||
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| Title | Yeast pre-60S Domain II intermediate | ||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / preLSU / preribosome / complex / Noc2-TAP particle | ||||||||||||||||||||||||
| Function / homology | Function and homology informationNoc1p-Noc2p complex / Noc2p-Noc3p complex / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of 5.8S rRNA / preribosome, small subunit precursor / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / preribosome, large subunit precursor / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) ...Noc1p-Noc2p complex / Noc2p-Noc3p complex / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of 5.8S rRNA / preribosome, small subunit precursor / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / preribosome, large subunit precursor / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / L13a-mediated translational silencing of Ceruloplasmin expression / maturation of LSU-rRNA / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / macroautophagy / rRNA processing / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / structural constituent of ribosome / ribosome / mRNA binding / nucleolus / mitochondrion / RNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||||||||||||||
Authors | Grundmann, L. / Gerhalter, M. / Prattes, M. / Grishkovskaya, I. / Kotisch, H. / Haselbach, D. / Bergler, H. | ||||||||||||||||||||||||
| Funding support | Austria, 1items
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Citation | Journal: To Be PublishedTitle: A comprehensive view on r- protein binding and rRNA domain structuring during early ribosome formation Authors: Gerhalter, M. / Prattes, M. / Grundmann, L. / Grishkovskaya, I. / Semarari, E.F. / Zisser, G. / Harald, K. / Merl-Pharm, J. / Hauck, S.M. / Haselbach, D. / Bergler, H. | ||||||||||||||||||||||||
| History |
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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 | 9qjc.cif.gz | 2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9qjc.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 9qjc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qj/9qjc ftp://data.pdbj.org/pub/pdb/validation_reports/qj/9qjc | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53201MC 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
-Protein , 5 types, 5 molecules 56DzB
| #1: Protein | Mass: 116832.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Protein | Mass: 81719.289 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: NOC2, YOR206W, YOX001 / Production host: ![]() |
| #4: Protein | Mass: 35754.605 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: ...Details: MSDEIVWQVINQSFCSHRIKAPNGQNFCRNEYNVTGLCTRQSCPLANSKYATVKCDNGKLYLYMKTPERAHTPAKLWERIKLSKNYTKALQQIDEHLLHWSKFFRHKCKQRFTKLTQVMITERRLALREEERHYVGVAPKVKRREQNRERKALVAAKIEKAIEKELMDRLKSGAYGDKPLNVDEKVWKKIMGQMEEENSQDEEEDWDEEEESDDGEVEYVADDGEGEYVDVDDLEKWLADSDREASSASESESDSESESDSDSDEENKNSAKRRKKGTSAKTKRPKVEIEYEEEHEVQNAEQEVAQ Source: (gene. exp.) ![]() Gene: MAK16, YAL025C / Production host: ![]() |
| #13: Protein | Mass: 33250.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RRP1, YDR087C, D4478 / Production host: ![]() |
| #16: Protein | Mass: 77972.430 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: NOP4, NOP77, YPL043W / Production host: ![]() |
-60S ribosomal protein ... , 9 types, 9 molecules CEFMOQSef
| #3: Protein | Mass: 39159.125 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL4A, RPL2, RPL2A, YBR031W, YBR0315 / Production host: ![]() |
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| #5: Protein | Mass: 20000.564 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL6A, RPL17A, YL16A, YML073C / Production host: ![]() |
| #6: Protein | Mass: 27686.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL7A, RPL6A, RPL8A, YL8A, YGL076C / Production host: ![]() |
| #7: Protein | Mass: 15195.066 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL14A, YKL006W, YKL153 / Production host: ![]() |
| #8: Protein | Mass: 22247.227 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL16A, RPL13, RPL21A, YIL133C / Production host: ![]() |
| #9: Protein | Mass: 20609.252 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL18A, RP28A, YOL120C / Production host: ![]() |
| #10: Protein | Mass: 20478.852 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL20A, RPL18A, RPL18A2, YMR242C, YM9408.04C / Production host: ![]() |
| #11: Protein | Mass: 14809.441 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL32, YBL092W, YBL0838 / Production host: ![]() |
| #12: Protein | Mass: 12177.130 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RPL33A, RPL37A, YPL143W, LPI4W, P2625 / Production host: ![]() |
-RNA chain , 2 types, 2 molecules 12
| #14: RNA chain | Mass: 1097493.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
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| #15: RNA chain | Mass: 51012.129 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
-Details
| Has protein modification | 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: Yeast pre-60S Domain II / Type: RIBOSOME Details: Noc2-TAP particle from yeast after Rpl7 depletion, where only Domain II adopts a structured conformation Entity ID: all / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R3.5/1 |
| Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 70 % / Chamber temperature: 4 K |
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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: 4000 nm / Nominal defocus min: 2000 nm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 11250 |
| Image scans | Width: 4096 / Height: 4096 |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 54106 / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 92.06 Å2 | ||||||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN