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Yorodumi- PDB-7pd3: Structure of the human mitoribosomal large subunit in complex wit... -
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Basic information
| Entry | Database: PDB / ID: 7pd3 | |||||||||||||||||||||||||||||||||||||||
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| Title | Structure of the human mitoribosomal large subunit in complex with NSUN4.MTERF4.GTPBP7 and MALSU1.L0R8F8.mt-ACP | |||||||||||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / mitochondrial ribosome / large subunit / ribosome biogenesis / GTPase / rRNA modification | |||||||||||||||||||||||||||||||||||||||
| 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 / iron-sulfur cluster assembly complex ...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 / iron-sulfur cluster assembly complex / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / protein-RNA adaptor activity / Complex I biogenesis / positive regulation of mitochondrial translation / RNA methyltransferase activity / Respiratory electron transport / rRNA methyltransferase activity / rRNA import into mitochondrion / rescue of stalled mitochondrial ribosome / mitochondrial translational termination / RNA folding chaperone / mitochondrial translational elongation / translation release factor activity, codon nonspecific / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / mitochondrial large ribosomal subunit assembly / 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 / fatty acid binding / aerobic respiration / 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 / negative regulation of translation / mitochondrial inner membrane / 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 / mitochondrion / : / RNA binding / nucleoplasm / nucleus Similarity search - Function | |||||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||||||||||||||||||||||||||||||||
Authors | Chandrasekaran, V. / Desai, N. / Burton, N.O. / Yang, H. / Price, J. / Miska, E.A. / Ramakrishnan, V. | |||||||||||||||||||||||||||||||||||||||
| Funding support | United Kingdom, 2items
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Citation | Journal: Elife / Year: 2021Title: Visualizing formation of the active site in the mitochondrial ribosome. Authors: Viswanathan Chandrasekaran / Nirupa Desai / Nicholas O Burton / Hanting Yang / Jon Price / Eric A Miska / V Ramakrishnan / ![]() Abstract: Ribosome assembly is an essential and conserved process that is regulated at each step by specific factors. Using cryo-electron microscopy (cryo-EM), we visualize the formation of the conserved ...Ribosome assembly is an essential and conserved process that is regulated at each step by specific factors. Using cryo-electron microscopy (cryo-EM), we visualize the formation of the conserved peptidyl transferase center (PTC) of the human mitochondrial ribosome. The conserved GTPase GTPBP7 regulates the correct folding of 16S ribosomal RNA (rRNA) helices and ensures 2'-O-methylation of the PTC base U3039. GTPBP7 binds the RNA methyltransferase NSUN4 and MTERF4, which sequester H68-71 of the 16S rRNA and allow biogenesis factors to access the maturing PTC. Mutations that disrupt binding of their orthologs to the large subunit potently activate mitochondrial stress and cause viability, development, and sterility defects. Next-generation RNA sequencing reveals widespread gene expression changes in these mutant animals that are indicative of mitochondrial stress response activation. We also answer the long-standing question of why NSUN4, but not its enzymatic activity, is indispensable for mitochondrial protein synthesis. | |||||||||||||||||||||||||||||||||||||||
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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 | 7pd3.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7pd3.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7pd3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pd/7pd3 ftp://data.pdbj.org/pub/pdb/validation_reports/pd/7pd3 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 13329MC 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
+39S ribosomal protein ... , 47 types, 48 molecules 0123456789CHDEFGJKLMNOPQRSTUVW...
-RNA chain , 2 types, 2 molecules AB
| #11: RNA chain | Mass: 557045.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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| #12: RNA chain | Mass: 22022.131 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1485738021 |
-Protein , 7 types, 7 molecules opqvwyx
| #48: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BQC6 |
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| #49: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q14197, peptidyl-tRNA hydrolase |
| #50: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / 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) / 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) / References: UniProt: O14561 |
| #57: Protein | Mass: 44012.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q7Z6M4 |
| #58: Protein | Mass: 43140.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: Q96CB9, Transferases; Transferring one-carbon groups; Methyltransferases |
-Protein/peptide , 1 types, 1 molecules t
| #53: Protein/peptide | Mass: 2400.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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-Mitochondrial ... , 2 types, 2 molecules uz
| #54: Protein | Mass: 26203.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EH3 |
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| #59: Protein | Mass: 37292.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BT17 |
-Non-polymers , 5 types, 97 molecules 








| #60: Chemical | | #61: Chemical | ChemComp-MG / #62: Chemical | ChemComp-PNS / | #63: Chemical | ChemComp-SAM / | #64: Chemical | |
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-Details
| Has protein modification | 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 mitoribosomal large subunit assembly intermediate Type: RIBOSOME / Entity ID: #1-#10, #12-#59 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 1.1 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 66340 / Symmetry type: POINT |
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About Yorodumi



Homo sapiens (human)
United Kingdom, 2items
Citation
UCSF Chimera










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