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Yorodumi- PDB-7of5: Structure of a human mitochondrial ribosome large subunit assembl... -
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Basic information
| Entry | Database: PDB / ID: 7of5 | ||||||||||||||||||
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| Title | Structure of a human mitochondrial ribosome large subunit assembly intermediate in complex with MTERF4-NSUN4 and GTPBP5 (dataset2). | ||||||||||||||||||
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Keywords | RIBOSOME / Mitochondria / Biogenesis / GTPase / NSUN4 / MTERF4 | ||||||||||||||||||
| Function / homology | Function and homology informationmitochondrial ribosomal large subunit rRNA binding / regulation of respiratory system process / rRNA modification in the mitochondrion / mitochondrial RNA modification / mRNA (cytidine-5-)-methyltransferase activity / regulation of mitochondrial translation / negative regulation of mitochondrial translation / mitochondrial RNA catabolic process / rRNA (cytosine-C5-)-methyltransferase activity / negative regulation of ribosome biogenesis ...mitochondrial ribosomal large subunit rRNA binding / regulation of respiratory system process / rRNA modification in the mitochondrion / mitochondrial RNA modification / mRNA (cytidine-5-)-methyltransferase activity / regulation of mitochondrial translation / negative regulation of mitochondrial translation / mitochondrial RNA catabolic process / rRNA (cytosine-C5-)-methyltransferase activity / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / protein-RNA adaptor activity / Protein lipoylation / Complex I biogenesis / positive regulation of mitochondrial translation / RNA methyltransferase activity / Respiratory electron transport / mitochondrial large ribosomal subunit assembly / rRNA methyltransferase activity / rRNA import into mitochondrion / rescue of stalled mitochondrial ribosome / mitochondrial translational termination / RNA folding chaperone / mitochondrial translational elongation / iron-sulfur cluster assembly complex / translation release factor activity, codon nonspecific / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / protein lipoylation / mitochondrial fission / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / rRNA methylation / mitochondrial ribosome / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / mitochondrial translation / iron-sulfur cluster assembly / ribosomal large subunit binding / mitochondrial electron transport, NADH to ubiquinone / proton motive force-driven mitochondrial ATP synthesis / acyl binding / mitochondrial respiratory chain complex I assembly / respiratory chain complex I / anatomical structure morphogenesis / acyl carrier activity / RNA processing / Mitochondrial protein degradation / Transferases; Transferring one-carbon groups; Methyltransferases / aerobic respiration / fatty acid binding / methyltransferase activity / ribosomal large subunit biogenesis / mitochondrial membrane / fatty acid biosynthetic process / rRNA processing / regulation of translation / double-stranded RNA binding / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / mitochondrial inner membrane / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / mRNA binding / GTPase activity / calcium ion binding / apoptotic process / GTP binding / structural molecule activity / magnesium ion binding / mitochondrion / : / RNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||||||||||||||
Authors | Hillen, H.S. / Lavdovskaia, E. / Nadler, F. / Hanitsch, E. / Linden, A. / Bohnsack, K.E. / Urlaub, H. / Richter-Dennerlein, R. | ||||||||||||||||||
| Funding support | Germany, 5items
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Citation | Journal: Nat Commun / Year: 2021Title: Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling. Authors: Hauke S Hillen / Elena Lavdovskaia / Franziska Nadler / Elisa Hanitsch / Andreas Linden / Katherine E Bohnsack / Henning Urlaub / Ricarda Richter-Dennerlein / ![]() Abstract: Ribosome biogenesis requires auxiliary factors to promote folding and assembly of ribosomal proteins and RNA. Particularly, maturation of the peptidyl transferase center (PTC) is mediated by ...Ribosome biogenesis requires auxiliary factors to promote folding and assembly of ribosomal proteins and RNA. Particularly, maturation of the peptidyl transferase center (PTC) is mediated by conserved GTPases, but the molecular basis is poorly understood. Here, we define the mechanism of GTPase-driven maturation of the human mitochondrial large ribosomal subunit (mtLSU) using endogenous complex purification, in vitro reconstitution and cryo-EM. Structures of transient native mtLSU assembly intermediates that accumulate in GTPBP6-deficient cells reveal how the biogenesis factors GTPBP5, MTERF4 and NSUN4 facilitate PTC folding. Addition of recombinant GTPBP6 reconstitutes late mtLSU biogenesis in vitro and shows that GTPBP6 triggers a molecular switch and progression to a near-mature PTC state. Additionally, cryo-EM analysis of GTPBP6-treated mature mitochondrial ribosomes reveals the structural basis for the dual-role of GTPBP6 in ribosome biogenesis and recycling. Together, these results provide a framework for understanding step-wise PTC folding as a critical conserved quality control checkpoint. #1: Journal: Biorxiv / Year: 2021Title: Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling Authors: Hillen, H.S. / Lavdovskaia, E. / Nadler, F. / Hanitsch, E. / Linden, A. / Bohnsack, K.E. / Urlaub, H. / Richter-Dennerlein, R. | ||||||||||||||||||
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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 | 7of5.cif.gz | 2.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7of5.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7of5.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/of/7of5 ftp://data.pdbj.org/pub/pdb/validation_reports/of/7of5 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 12870MC ![]() 7of0C ![]() 7of2C ![]() 7of3C ![]() 7of4C ![]() 7of6C ![]() 7of7C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
+39S ribosomal protein ... , 46 types, 46 molecules 0123456789DEFHIJKLMNOPQRSTUVWX...
-RNA chain , 1 types, 1 molecules A
| #11: RNA chain | Mass: 500061.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / Strain: HEK293-Flp-In T-Rex |
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-Mitochondrial ... , 3 types, 3 molecules Bux
| #12: RNA chain | Mass: 22022.131 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: GenBank: 1485738021 |
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| #54: Protein | Mass: 26203.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: Q96EH3 |
| #57: Protein | Mass: 44018.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: Q9H4K7 |
-Protein , 7 types, 7 molecules CGopqvw
| #13: Protein | Mass: 43140.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/-References: UniProt: Q96CB9, Transferases; Transferring one-carbon groups; Methyltransferases |
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| #17: Protein | Mass: 44012.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: Q7Z6M4 |
| #49: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: Q9BQC6 |
| #50: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: Q14197, peptidyl-tRNA hydrolase |
| #51: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: Q8TAE8 |
| #55: Protein | Mass: 8460.787 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: L0R8F8 |
| #56: Protein | Mass: 17434.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Variant: GTPBP6 -/- / References: UniProt: O14561 |
-Non-polymers , 3 types, 75 molecules 




| #58: Chemical | | #59: Chemical | ChemComp-MG / #60: Chemical | |
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-Details
| Has ligand of interest | Y |
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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: Human mitochondrial ribosome large subunit assembly intermediate in complex with MTERF4-NSUN4 and GTPBP5 (dataset2). Type: RIBOSOME / Entity ID: #1-#57 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) / Strain: HEK293-Flp-In T-Rex / Organelle: Mitochondria |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid type: Quantifoil R3.5/1 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Calibrated defocus min: 300 nm / Calibrated defocus max: 2100 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 37 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
| EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 2983982 | |||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 36934 / Symmetry type: POINT | |||||||||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | |||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 5OOL Accession code: 5OOL / Source name: PDB / Type: experimental model |
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About Yorodumi



Homo sapiens (human)
Germany, 5items
Citation
UCSF Chimera




















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