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- PDB-9hcf: 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: 9hcf | ||||||||||||
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Title | Mouse mitoribosome large subunit assembly intermediate bound to NSUN4, METRF4, GTPBP7, GTPBP10 and the MALSU-L0R8F8-mtACP complex with uL16m, State B2 (SAMC knock-out) | ||||||||||||
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![]() | RIBOSOME / mitochondria / ribosome assembly / large subunit | ||||||||||||
Function / homology | ![]() Mitochondrial translation elongation / Mitochondrial translation termination / mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation ...Mitochondrial translation elongation / Mitochondrial translation termination / mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / positive regulation of mitochondrial translation / rRNA import into mitochondrion / Respiratory electron transport / mitochondrial transcription / mitochondrial translational termination / : / mitochondrial translational elongation / ribonuclease III activity / translation release factor activity, codon nonspecific / Mitochondrial protein degradation / camera-type eye development / mitochondrial [2Fe-2S] assembly complex / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit / mitochondrial fission / mitochondrial large ribosomal subunit binding / peptidyl-tRNA hydrolase / rRNA methylation / mitochondrial ribosome / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / mitochondrial translation / protein targeting to mitochondrion / iron-sulfur cluster assembly / mitochondrial respiratory chain complex I assembly / proton motive force-driven mitochondrial ATP synthesis / respiratory chain complex I / RNA processing / rescue of stalled ribosome / cellular response to leukemia inhibitory factor / aerobic respiration / Transferases; Transferring one-carbon groups; Methyltransferases / ribosome assembly / ribosomal large subunit biogenesis / cytosolic ribosome assembly / rRNA processing / fatty acid biosynthetic process / cell junction / ribosome biogenesis / double-stranded RNA binding / heart development / 5S rRNA binding / double-stranded DNA binding / small ribosomal subunit rRNA binding / mitochondrial inner membrane / rRNA binding / nuclear body / structural constituent of ribosome / mitochondrial matrix / protein domain specific binding / translation / ribonucleoprotein complex / nucleotide binding / GTPase activity / apoptotic process / regulation of DNA-templated transcription / GTP binding / nucleolus / 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: 2.85 Å | ||||||||||||
![]() | Singh, V. / Rorbach, J. / Freyer, C. / Amunts, A. / Wredenberg, A. | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: 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. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.7 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.3 MB | Display | ![]() |
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Full document | ![]() | 2.4 MB | Display | |
Data in XML | ![]() | 252.3 KB | Display | |
Data in CIF | ![]() | 414.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 52047MC ![]() 9hccC ![]() 9hcdC ![]() 9hceC ![]() 9hcgC ![]() 9hchC ![]() 9e9c M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 508609.969 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 ... , 50 types, 50 molecules DEFHIJKLMNOPQRSTUVWXYZ123467bf...
-Protein , 5 types, 5 molecules xvywt
#25: 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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#42: Protein | Mass: 8444.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#50: Protein | Mass: 40306.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#51: Protein | Mass: 17390.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#59: Protein | Mass: 40200.605 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Mitochondrial ... , 2 types, 2 molecules uz
#41: Protein | Mass: 26055.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#48: Protein | Mass: 36732.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 4 types, 104 molecules 






#60: Chemical | ChemComp-MG / #61: Chemical | ChemComp-FES / | #62: Chemical | #63: 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, #25, #4-#5, #9-#11, #14-#19, #21-#22, #26-#47, #7, #48-#50, #3, #12, #51-#54, #6, #23, #13, #55-#56, #24, #57-#58, #20, #8, #59, #2 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: ![]() |
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: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 55461 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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