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Yorodumi- PDB-7oic: Cryo-EM structure of late human 39S mitoribosome assembly interme... -
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Basic information
| Entry | Database: PDB / ID: 7oic | ||||||
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| Title | Cryo-EM structure of late human 39S mitoribosome assembly intermediates, state 4 | ||||||
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Keywords | RIBOSOME / 39S mitoribosome / ribosome biogenesis | ||||||
| Function / homology | Function and homology informationmRNA (cytidine-5-)-methyltransferase activity / rRNA modification in the mitochondrion / mitochondrial RNA modification / mitochondrial RNA catabolic process / negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / rRNA (cytosine-C5-)-methyltransferase activity / protein lipoylation / negative regulation of ribosome biogenesis / Complex I biogenesis ...mRNA (cytidine-5-)-methyltransferase activity / rRNA modification in the mitochondrion / mitochondrial RNA modification / mitochondrial RNA catabolic process / negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / rRNA (cytosine-C5-)-methyltransferase activity / protein lipoylation / negative regulation of ribosome biogenesis / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / positive regulation of mitochondrial translation / Respiratory electron transport / rRNA import into mitochondrion / RNA methyltransferase activity / rRNA methyltransferase activity / mitochondrial translational termination / mitochondrial transcription / mitochondrial ribosome assembly / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / 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 / mitochondrial ribosome / mitochondrial small ribosomal subunit / rRNA methylation / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / peptidyl-tRNA hydrolase activity / mitochondrial translation / [2Fe-2S] cluster assembly / protein targeting to mitochondrion / iron-sulfur cluster assembly / acyl binding / acyl carrier activity / ribosomal large subunit binding / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / proton motive force-driven mitochondrial ATP synthesis / respiratory chain complex I / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled ribosome / aerobic respiration / Transferases; Transferring one-carbon groups; Methyltransferases / cellular response to leukemia inhibitory factor / fatty acid binding / ribosomal large subunit biogenesis / methyltransferase activity / mitochondrial membrane / fibrillar center / rRNA processing / fatty acid biosynthetic process / cell junction / double-stranded RNA binding / heart development / 5S rRNA binding / small ribosomal subunit rRNA binding / double-stranded DNA 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 / mRNA binding / apoptotic process / calcium ion binding / regulation of DNA-templated transcription / nucleolus / structural molecule activity / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||
Authors | Cheng, J. / Berninghausen, O. / Beckmann, R. | ||||||
Citation | Journal: Nat Commun / Year: 2021Title: A distinct assembly pathway of the human 39S late pre-mitoribosome. Authors: Jingdong Cheng / Otto Berninghausen / Roland Beckmann / ![]() Abstract: Assembly of the mitoribosome is largely enigmatic and involves numerous assembly factors. Little is known about their function and the architectural transitions of the pre-ribosomal intermediates. ...Assembly of the mitoribosome is largely enigmatic and involves numerous assembly factors. Little is known about their function and the architectural transitions of the pre-ribosomal intermediates. Here, we solve cryo-EM structures of the human 39S large subunit pre-ribosomes, representing five distinct late states. Besides the MALSU1 complex used as bait for affinity purification, we identify several assembly factors, including the DDX28 helicase, MRM3, GTPBP10 and the NSUN4-mTERF4 complex, all of which keep the 16S rRNA in immature conformations. The late transitions mainly involve rRNA domains IV and V, which form the central protuberance, the intersubunit side and the peptidyltransferase center of the 39S subunit. Unexpectedly, we find deacylated tRNA in the ribosomal E-site, suggesting a role in 39S assembly. Taken together, our study provides an architectural inventory of the distinct late assembly phase of the human 39S mitoribosome. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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| PDBx/mmCIF format | 7oic.cif.gz | 2.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7oic.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7oic.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7oic_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 7oic_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 7oic_validation.xml.gz | 197.9 KB | Display | |
| Data in CIF | 7oic_validation.cif.gz | 318.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oi/7oic ftp://data.pdbj.org/pub/pdb/validation_reports/oi/7oic | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 12925MC ![]() 7oi6C ![]() 7oi7C ![]() 7oi8C ![]() 7oi9C ![]() 7oiaC ![]() 7oibC ![]() 7oidC ![]() 7oieC 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
-RNA chain , 2 types, 2 molecules AB
| #1: RNA chain | Mass: 500043.594 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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| #2: 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 |
+39S ribosomal protein ... , 47 types, 47 molecules DEFHIJKLMNOPQRSTUVWXYZ01234567...
-Protein , 8 types, 8 molecules opquvwxy
| #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 |
| #53: Protein | Mass: 26203.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EH3 |
| #54: Protein | Mass: 8460.787 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: L0R8F8 |
| #55: Protein | Mass: 17434.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14561 |
| #56: Protein | Mass: 43187.367 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 |
| #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 |
-Non-polymers , 6 types, 83 molecules 










| #58: Chemical | ChemComp-MG / #59: Chemical | ChemComp-C / | #60: Chemical | ChemComp-A / | #61: Chemical | #62: Chemical | ChemComp-PNS / | #63: Chemical | ChemComp-SAM / | |
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-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: Human 39S mitoribosome assembly intermediates, state 4 Type: RIBOSOME / Entity ID: #1-#57 / Source: NATURAL |
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| 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: 28 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 83176 / Symmetry type: POINT |
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