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Yorodumi- PDB-8pk0: human mitoribosomal large subunit assembly intermediate 1 with GT... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8pk0 | ||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | human mitoribosomal large subunit assembly intermediate 1 with GTPBP10-GTPBP7 | ||||||||||||||||||||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / mitochondria / maturation / biogenesis / GTPBP7 / GTPBP10 / GTP Binding Protein 10 / OBGH2 / MTG1 / LSU | ||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationmRNA (cytidine-5-)-methyltransferase activity / rRNA modification in the mitochondrion / regulation of respiratory system process / mitochondrial RNA modification / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / rRNA (cytosine-C5-)-methyltransferase activity / mitochondrial large ribosomal subunit assembly / negative regulation of ribosome biogenesis ...mRNA (cytidine-5-)-methyltransferase activity / rRNA modification in the mitochondrion / regulation of respiratory system process / mitochondrial RNA modification / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / rRNA (cytosine-C5-)-methyltransferase activity / mitochondrial large ribosomal subunit assembly / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / positive regulation of mitochondrial translation / Complex I biogenesis / RNA methyltransferase activity / Respiratory electron transport / protein lipoylation / rRNA methyltransferase activity / rRNA import into mitochondrion / mitochondrial transcription / mitochondrial translational termination / Mitochondrial ribosome-associated quality control / mitochondrial translational elongation / mitochondrial ribosome assembly / Mitochondrial translation elongation / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / Mitochondrial translation termination / camera-type eye development / mitochondrial fission / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial [2Fe-2S] assembly complex / translation release factor activity / mitochondrial ribosome / rRNA methylation / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / mitochondrial translation / : / iron-sulfur cluster assembly / acyl binding / acyl carrier activity / ribosomal large subunit binding / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled cytosolic ribosome / Transferases; Transferring one-carbon groups; Methyltransferases / fatty acid binding / aerobic respiration / cellular response to leukemia inhibitory factor / ribosomal large subunit biogenesis / methyltransferase activity / mitochondrial membrane / fibrillar center / fatty acid biosynthetic process / rRNA processing / cell junction / double-stranded RNA binding / chromosome / heart development / 5S rRNA binding / double-stranded DNA binding / small ribosomal subunit rRNA 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 / GTPase activity / mRNA binding / apoptotic process / calcium ion binding / regulation of DNA-templated transcription / GTP binding / nucleolus / structural molecule activity / magnesium ion binding / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å | ||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Kummer, E. / Nguyen, T.G. / Ritter, C. | ||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | Denmark, 1items
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Citation | Journal: Nat Commun / Year: 2023Title: Structural insights into the role of GTPBP10 in the RNA maturation of the mitoribosome. Authors: Thu Giang Nguyen / Christina Ritter / Eva Kummer / ![]() Abstract: Mitochondria contain their own genetic information and a dedicated translation system to express it. The mitochondrial ribosome is assembled from mitochondrial-encoded RNA and nuclear-encoded ...Mitochondria contain their own genetic information and a dedicated translation system to express it. The mitochondrial ribosome is assembled from mitochondrial-encoded RNA and nuclear-encoded ribosomal proteins. Assembly is coordinated in the mitochondrial matrix by biogenesis factors that transiently associate with the maturing particle. Here, we present a structural snapshot of a large mitoribosomal subunit assembly intermediate containing 7 biogenesis factors including the GTPases GTPBP7 and GTPBP10. Our structure illustrates how GTPBP10 aids the folding of the ribosomal RNA during the biogenesis process, how this process is related to bacterial ribosome biogenesis, and why mitochondria require two biogenesis factors in contrast to only one in bacteria. | ||||||||||||||||||||||||||||||||||||||||||||||||
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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 | 8pk0.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8pk0.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8pk0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pk/8pk0 ftp://data.pdbj.org/pub/pdb/validation_reports/pk/8pk0 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 17719MC ![]() 8qsjC 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
+39S ribosomal protein ... , 45 types, 45 molecules 0T1U2V3W5X6Y7Z8a9cdDeEfFgHhIiJ...
-Mitochondrial ... , 2 types, 2 molecules uz
| #3: 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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| #18: Protein | Mass: 37292.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BT17 |
-Protein , 9 types, 9 molecules vwxybopqt
| #6: Protein | Mass: 8460.787 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: L0R8F8 |
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| #9: Protein | Mass: 17434.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14561 |
| #12: 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 |
| #15: Protein | Mass: 44012.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q7Z6M4 |
| #24: Protein | Mass: 23352.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N983 |
| #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 |
| #50: 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 |
| #52: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8TAE8 |
| #58: Protein | Mass: 42996.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: A4D1E9 |
-RNA chain , 2 types, 2 molecules AB
| #25: RNA chain | Mass: 509550.594 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1858624182 |
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| #27: RNA chain | Mass: 22961.699 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1896813692 |
-Non-polymers , 6 types, 111 molecules 










| #59: Chemical | ChemComp-ZN / | ||||
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| #60: Chemical | ChemComp-PM8 / | ||||
| #61: Chemical | ChemComp-SAM / | ||||
| #62: Chemical | | #63: Chemical | ChemComp-MG / #64: Chemical | ChemComp-K / |
-Details
| Has ligand of interest | Y |
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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: large mitoribosomal subunit biogenesis intermediate with GTPBP10, GTPBP7, NSUN4-MTERF4, ACP-module Type: RIBOSOME Entity ID: #1, #4, #7, #10, #13, #16, #19, #21, #23, #27, #29, #31, #33, #35, #37, #39, #41, #43, #45, #47, #49, #51, #53, #55, #57, #2, #5, #8, #11, #14, #17, #20, #22, #26, #28, #30, #32, #34, #36, ...Entity ID: #1, #4, #7, #10, #13, #16, #19, #21, #23, #27, #29, #31, #33, #35, #37, #39, #41, #43, #45, #47, #49, #51, #53, #55, #57, #2, #5, #8, #11, #14, #17, #20, #22, #26, #28, #30, #32, #34, #36, #38, #40, #42, #44, #46, #48, #50, #52, #54, #56, #58, #3, #6, #9, #12, #15, #18 Source: NATURAL |
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| Molecular weight | Value: 1.9 MDa / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.6 |
| 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 / Nominal defocus max: 2500 nm / Nominal defocus min: 700 nm |
| Image recording | Electron dose: 40 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.19.2_4158: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 31656 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
Denmark, 1items
Citation



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FIELD EMISSION GUN