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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 informationmitochondrial ribosomal large subunit rRNA binding / 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 / regulation of mitochondrial transcription / rRNA (cytosine-C5-)-methyltransferase activity ...mitochondrial ribosomal large subunit rRNA binding / 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 / regulation of mitochondrial transcription / rRNA (cytosine-C5-)-methyltransferase activity / protein-RNA adaptor activity / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / positive regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / Complex I biogenesis / Respiratory electron transport / RNA methyltransferase activity / rRNA methyltransferase activity / rRNA import into mitochondrion / RNA folding chaperone / mitochondrial translational termination / mitochondrial translational elongation / mitochondrial ribosome assembly / translation release factor activity, codon nonspecific / Mitochondrial translation elongation / Mitochondrial translation initiation / camera-type eye development / Mitochondrial ribosome-associated quality control / protein lipoylation / mitochondrial fission / iron-sulfur cluster assembly complex / Mitochondrial translation termination / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / 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 / mitochondrial electron transport, NADH to ubiquinone / acyl binding / mitochondrial respiratory chain complex I assembly / respiratory chain complex I / anatomical structure morphogenesis / acyl carrier activity / RNA processing / Mitochondrial protein degradation / rescue of stalled cytosolic ribosome / Transferases; Transferring one-carbon groups; Methyltransferases / aerobic respiration / fatty acid binding / 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 / small ribosomal subunit rRNA binding / endonuclease activity / 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 / hydrolase activity / mRNA binding / GTPase activity / apoptotic process / calcium ion binding / GTP binding / nucleolus / structural molecule activity / magnesium ion binding / mitochondrion / : / RNA binding / nucleoplasm / nucleus / plasma membrane 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