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Yorodumi- PDB-7odt: State C of the human mitoribosomal large subunit assembly intermediate -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7odt | ||||||||||||
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| Title | State C of the human mitoribosomal large subunit assembly intermediate | ||||||||||||
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Keywords | RIBOSOME / mitoribosome / assembly intermediate / large subunit / LSU / mt-LSU | ||||||||||||
| Function / homology | Function and homology informationmRNA (cytidine-5-)-methyltransferase activity / rRNA modification in the mitochondrion / regulation of respiratory system process / mitochondrial RNA modification / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / rRNA (cytosine-C5-)-methyltransferase activity / mitochondrial large ribosomal subunit assembly / negative regulation of ribosome biogenesis ...mRNA (cytidine-5-)-methyltransferase activity / rRNA modification in the mitochondrion / regulation of respiratory system process / mitochondrial RNA modification / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / rRNA (cytosine-C5-)-methyltransferase activity / mitochondrial large ribosomal subunit assembly / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / protein lipoylation / positive regulation of mitochondrial translation / Complex I biogenesis / RNA methyltransferase activity / Respiratory electron transport / rRNA methyltransferase activity / rRNA import into mitochondrion / mitochondrial transcription / mitochondrial translational termination / Mitochondrial ribosome-associated quality control / mitochondrial translational elongation / mitochondrial ribosome assembly / Mitochondrial translation elongation / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / Mitochondrial translation termination / camera-type eye development / mitochondrial fission / iron-sulfur cluster assembly complex / translation release factor activity / mitochondrial large ribosomal subunit binding / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial [2Fe-2S] assembly complex / mitochondrial ribosome / rRNA methylation / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / mitochondrial translation / : / iron-sulfur cluster assembly / acyl binding / acyl carrier activity / ribosomal large subunit binding / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled cytosolic ribosome / Transferases; Transferring one-carbon groups; Methyltransferases / fatty acid binding / aerobic respiration / cellular response to leukemia inhibitory factor / ribosomal large subunit biogenesis / methyltransferase activity / mitochondrial membrane / fibrillar center / fatty acid biosynthetic process / rRNA processing / cell junction / double-stranded RNA binding / heart development / 5S rRNA binding / double-stranded DNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / mitochondrial inner membrane / negative regulation of translation / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / GTPase activity / mRNA binding / apoptotic process / calcium ion binding / regulation of DNA-templated transcription / GTP binding / nucleolus / structural molecule activity / magnesium ion binding / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / plasma membrane Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
Authors | Lenarcic, T. / Jaskolowski, M. / Leibundgut, M. / Scaiola, A. / Schoenhut, T. / Saurer, M. / Lee, R.G. / Rackham, O. / Filipovska, A. / Ban, N. | ||||||||||||
| Funding support | Switzerland, 3items
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Citation | Journal: Nat Commun / Year: 2021Title: Stepwise maturation of the peptidyl transferase region of human mitoribosomes. Authors: Tea Lenarčič / Mateusz Jaskolowski / Marc Leibundgut / Alain Scaiola / Tanja Schönhut / Martin Saurer / Richard G Lee / Oliver Rackham / Aleksandra Filipovska / Nenad Ban / ![]() Abstract: Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral ...Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral bacterial ribosomes and feature dramatically reduced ribosomal RNAs. The structural basis of the mammalian mitochondrial ribosome assembly is currently not well understood. Here we present eight distinct assembly intermediates of the human large mitoribosomal subunit involving seven assembly factors. We discover that the NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by the MRM2 methyltransferase and quality control interactions with the conserved mitochondrial GTPase MTG2 that contacts the sarcin-ricin loop and the immature active site. The successive action of these factors leads to the formation of the peptidyl transferase active site of the mitoribosome and the folding of the surrounding rRNA regions responsible for interactions with tRNAs and the small ribosomal subunit. | ||||||||||||
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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 | 7odt.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7odt.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7odt.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/od/7odt ftp://data.pdbj.org/pub/pdb/validation_reports/od/7odt | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 12847MC ![]() 7odrC ![]() 7odsC 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
-Mitochondrial ... , 3 types, 3 molecules tuB
| #1: Protein | Mass: 44018.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: Q9H4K7 |
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| #2: Protein | Mass: 26203.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: Q96EH3 |
| #18: RNA chain | Mass: 22961.699 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA |
-Protein , 7 types, 7 molecules vwxyopq
| #3: Protein | Mass: 8460.787 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: L0R8F8 |
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| #4: Protein | Mass: 17434.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: O14561 |
| #5: Protein | Mass: 43140.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNAReferences: UniProt: Q96CB9, Transferases; Transferring one-carbon groups; Methyltransferases |
| #6: Protein | Mass: 44012.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: Q7Z6M4 |
| #54: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: Q9BQC6 |
| #55: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: Q14197, peptidyl-tRNA hydrolase |
| #56: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA / References: UniProt: Q8TAE8 |
+39S ribosomal protein ... , 47 types, 47 molecules 0123456789DEFHIJKLMNOPQRSTUVWX...
-RNA chain , 1 types, 1 molecules A
| #17: RNA chain | Mass: 500047.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK 293 EBNA |
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-Non-polymers , 7 types, 111 molecules 












| #59: Chemical | ChemComp-GDP / | ||||||||||
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| #60: Chemical | ChemComp-MG / #61: Chemical | ChemComp-PM8 / | #62: Chemical | ChemComp-SAM / | #63: Chemical | #64: Chemical | ChemComp-K / #65: Chemical | ChemComp-FES / | |
-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: State C of the human mitoribosomal large subunit assembly intermediate Type: RIBOSOME / Entity ID: #1-#58 / Source: NATURAL | ||||||||||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) / Strain: HEK 293 EBNA | ||||||||||||||||||||
| Buffer solution | pH: 7.6 | ||||||||||||||||||||
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/2 | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 277.15 K Details: 4 uL of the sample was blotted for 2-6 sec before plunging |
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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 / Cs: 2.7 mm / C2 aperture diameter: 100 µm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 62552 / Symmetry type: POINT |
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Homo sapiens (human)
Switzerland, 3items
Citation
UCSF Chimera



















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