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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 / 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 / Mitochondrial Fatty Acid Beta-Oxidation ...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 / Mitochondrial Fatty Acid Beta-Oxidation / positive regulation of mitochondrial translation / Protein lipoylation / negative regulation of ribosome biogenesis / Complex I biogenesis / RNA methyltransferase activity / Respiratory electron transport / protein-RNA adaptor activity / rRNA methyltransferase activity / rRNA import into mitochondrion / rescue of stalled mitochondrial ribosome / RNA folding chaperone / mitochondrial translational termination / mitochondrial translational elongation / translation release factor activity, codon nonspecific / mitochondrial ribosome assembly / Mitochondrial translation elongation / mitochondrial large ribosomal subunit assembly / Mitochondrial translation initiation / protein lipoylation / mitochondrial fission / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / rRNA methylation / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / mitochondrial translation / iron-sulfur cluster assembly / acyl carrier activity / 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 / RNA processing / Mitochondrial protein degradation / Transferases; Transferring one-carbon groups; Methyltransferases / fatty acid binding / aerobic respiration / ribosomal large subunit biogenesis / fatty acid biosynthetic process / mitochondrial membrane / rRNA processing / double-stranded RNA binding / large ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / negative regulation of translation / mitochondrial inner membrane / rRNA binding / chromosome / ribosome / translation / ribonucleoprotein complex / structural constituent of ribosome / mitochondrial matrix / apoptotic process / nucleotide binding / protein domain specific binding / GTPase activity / calcium ion binding / nucleolus / GTP binding / structural molecule activity / magnesium ion binding / mitochondrion / RNA binding / extracellular region / 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