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Yorodumi- PDB-9e9c: Mouse mitoribosome large subunit assembly intermediate bound to N... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9e9c | ||||||||||||
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| Title | Mouse mitoribosome large subunit assembly intermediate bound to NSUN4, METRF4, GTPBP7, GTPBP10 and the MALSU1-L0R8F8-mt-ACP complex (without uL16m), State B1 (SAMC knock-out) | ||||||||||||
Components |
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Keywords | RIBOSOME / mitochondria / ribosome assembly / large subunit | ||||||||||||
| Function / homology | Function and homology informationMitochondrial translation elongation / mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / mitochondrial small ribosomal subunit assembly / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / regulation of mitochondrial transcription / rRNA (cytosine-C5-)-methyltransferase activity / negative regulation of ribosome biogenesis ...Mitochondrial translation elongation / mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / mitochondrial small ribosomal subunit assembly / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / regulation of mitochondrial transcription / rRNA (cytosine-C5-)-methyltransferase activity / negative regulation of ribosome biogenesis / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / positive regulation of mitochondrial translation / Mitochondrial ribosome-associated quality control / mitochondrial large ribosomal subunit assembly / Mitochondrial translation termination / Respiratory electron transport / translation release factor activity / rRNA import into mitochondrion / mitochondrial translational termination / ribonuclease III activity / mitochondrial translational elongation / mitochondrial ribosome assembly / Mitochondrial protein degradation / translation release factor activity, codon nonspecific / camera-type eye development / protein lipoylation / mitochondrial fission / iron-sulfur cluster assembly complex / peptidyl-tRNA hydrolase / mitochondrial large ribosomal subunit / mitochondrial large ribosomal subunit binding / mitochondrial [2Fe-2S] assembly complex / mitochondrial ribosome / rRNA methylation / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / mitochondrial translation / [2Fe-2S] cluster assembly / iron-sulfur cluster assembly / ribosomal large subunit binding / proton motive force-driven mitochondrial ATP synthesis / acyl binding / mitochondrial respiratory chain complex I assembly / respiratory chain complex I / acyl carrier activity / RNA processing / cytosolic ribosome / rescue of stalled cytosolic ribosome / Transferases; Transferring one-carbon groups; Methyltransferases / aerobic respiration / cellular response to leukemia inhibitory factor / ribosomal large subunit biogenesis / mitochondrion organization / fibrillar center / rRNA processing / cell junction / double-stranded RNA binding / large ribosomal subunit / heart development / ribosome biogenesis / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / 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 / mRNA binding / GTPase activity / apoptotic process / GTP binding / nucleolus / structural molecule activity / magnesium ion binding / mitochondrion / RNA binding / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.62 Å | ||||||||||||
Authors | Singh, V. / Rorbach, J. / Freyer, C. / Amunts, A. / Wredenberg, A. | ||||||||||||
| Funding support | Sweden, Denmark, 3items
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Citation | Journal: Nat Commun / Year: 2025Title: The mitochondrial methylation potential gates mitoribosome assembly. Authors: Ruth I C Glasgow / Vivek Singh / Lucía Peña-Pérez / Alissa Wilhalm / Marco F Moedas / David Moore / Florian A Rosenberger / Xinping Li / Ilian Atanassov / Mira Saba / Miriam Cipullo / ...Authors: Ruth I C Glasgow / Vivek Singh / Lucía Peña-Pérez / Alissa Wilhalm / Marco F Moedas / David Moore / Florian A Rosenberger / Xinping Li / Ilian Atanassov / Mira Saba / Miriam Cipullo / Joanna Rorbach / Anna Wedell / Christoph Freyer / Alexey Amunts / Anna Wredenberg / ![]() Abstract: S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct ...S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct long-read RNA sequencing in mouse tissues and embryonic fibroblasts, we show that processing of the mitochondrial ribosomal gene cluster fails in the absence of mitochondrial SAM, leading to an accumulation of unprocessed precursors. Proteomic analysis of ribosome fractions revealed these precursors associated with processing and assembly factors, indicating stalled biogenesis. Structural analysis by cryo-electron microscopy demonstrated that SAM-dependent methylation is required for peptidyl transferase centre formation during mitoribosome assembly. Our findings identify a critical role for SAM in coordinating mitoribosomal RNA processing and large subunit maturation, linking cellular methylation potential to mitochondrial translation capacity. | ||||||||||||
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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 | 9e9c.cif.gz | 4.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9e9c.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9e9c.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e9/9e9c ftp://data.pdbj.org/pub/pdb/validation_reports/e9/9e9c | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 47791MC ![]() 9hccC ![]() 9hcdC ![]() 9hceC ![]() 9hcfC ![]() 9hcgC ![]() 9hchC 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
-RNA chain , 2 types, 2 molecules AB
| #1: RNA chain | Mass: 508601.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: RNA chain | Mass: 21862.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Large ribosomal subunit protein ... , 49 types, 49 molecules DEFHIJKLMOPQRSTUVWXYZ0123467bc...
-Protein , 5 types, 5 molecules xvwyt
| #24: Protein | Mass: 42904.293 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q9CZ57, Transferases; Transferring one-carbon groups; Methyltransferases |
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| #48: Protein | Mass: 8444.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 17390.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: Protein | Mass: 40306.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 40200.605 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Mitochondrial ... , 2 types, 2 molecules uz
| #47: Protein | Mass: 26055.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #55: Protein | Mass: 36732.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 4 types, 100 molecules 






| #59: Chemical | ChemComp-MG / #60: Chemical | #61: Chemical | ChemComp-FES / | #62: Chemical | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-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: mitoribosome large subunit assembly intermediate / Type: RIBOSOME Entity ID: #1-#2, #24, #3-#6, #9-#23, #25-#54, #7, #55-#57, #8, #58 Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| 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: 2000 nm / Nominal defocus min: 400 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.62 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 6503 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi





Sweden,
Denmark, 3items
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FIELD EMISSION GUN