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Yorodumi- PDB-8csu: Human mitochondrial small subunit assembly intermediate (State C*) -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8csu | |||||||||
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| Title | Human mitochondrial small subunit assembly intermediate (State C*) | |||||||||
Components |
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Keywords | RIBOSOME / Ribonucleoprotein complex / Mitochondria Biogenesis | |||||||||
| Function / homology | Function and homology informationmitochondrial small ribosomal subunit assembly / mitochondrial ribosome binding / rRNA modification in the mitochondrion / mitochondrial transcription factor activity / transcription initiation at mitochondrial promoter / rRNA modification / rRNA (adenine-N6,N6-)-dimethyltransferase activity / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination ...mitochondrial small ribosomal subunit assembly / mitochondrial ribosome binding / rRNA modification in the mitochondrion / mitochondrial transcription factor activity / transcription initiation at mitochondrial promoter / rRNA modification / rRNA (adenine-N6,N6-)-dimethyltransferase activity / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / Mitochondrial translation initiation / negative regulation of mitotic nuclear division / S-adenosyl-L-methionine binding / mitochondrial ribosome / mitochondrial small ribosomal subunit / rRNA methylation / mitochondrial translation / apoptotic mitochondrial changes / mitochondrial nucleoid / positive regulation of proteolysis / ribosomal small subunit binding / Mitochondrial protein degradation / Transferases; Transferring one-carbon groups; Methyltransferases / apoptotic signaling pathway / Transcriptional activation of mitochondrial biogenesis / rRNA processing / cell junction / regulation of translation / 4 iron, 4 sulfur cluster binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / nuclear membrane / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / tRNA binding / cell population proliferation / mitochondrial inner membrane / rRNA binding / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / protein domain specific binding / intracellular membrane-bounded organelle / mRNA binding / GTP binding / nucleolus / mitochondrion / DNA binding / RNA binding / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å | |||||||||
Authors | Harper, N.J. / Burnside, C. / Klinge, S. | |||||||||
| Funding support | United States, 2items
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Citation | Journal: Nature / Year: 2023Title: Principles of mitoribosomal small subunit assembly in eukaryotes. Authors: Nathan J Harper / Chloe Burnside / Sebastian Klinge / ![]() Abstract: Mitochondrial ribosomes (mitoribosomes) synthesize proteins encoded within the mitochondrial genome that are assembled into oxidative phosphorylation complexes. Thus, mitoribosome biogenesis is ...Mitochondrial ribosomes (mitoribosomes) synthesize proteins encoded within the mitochondrial genome that are assembled into oxidative phosphorylation complexes. Thus, mitoribosome biogenesis is essential for ATP production and cellular metabolism. Here we used cryo-electron microscopy to determine nine structures of native yeast and human mitoribosomal small subunit assembly intermediates, illuminating the mechanistic basis for how GTPases are used to control early steps of decoding centre formation, how initial rRNA folding and processing events are mediated, and how mitoribosomal proteins have active roles during assembly. Furthermore, this series of intermediates from two species with divergent mitoribosomal architecture uncovers both conserved principles and species-specific adaptations that govern the maturation of mitoribosomal small subunits in eukaryotes. By revealing the dynamic interplay between assembly factors, mitoribosomal proteins and rRNA that are required to generate functional subunits, our structural analysis provides a vignette for how molecular complexity and diversity can evolve in large ribonucleoprotein assemblies. | |||||||||
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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 | 8csu.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8csu.ent.gz | 1.2 MB | Display | PDB format |
| PDBx/mmJSON format | 8csu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8csu_validation.pdf.gz | 2 MB | Display | wwPDB validaton report |
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| Full document | 8csu_full_validation.pdf.gz | 2 MB | Display | |
| Data in XML | 8csu_validation.xml.gz | 174 KB | Display | |
| Data in CIF | 8csu_validation.cif.gz | 279.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/8csu ftp://data.pdbj.org/pub/pdb/validation_reports/cs/8csu | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 26971MC ![]() 8cspC ![]() 8csqC ![]() 8csrC ![]() 8cssC ![]() 8cstC ![]() 8d8jC ![]() 8d8kC ![]() 8d8lC 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
+28S ribosomal protein ... , 27 types, 27 molecules 01BCDEFGHIJKLMNOPQRSTUVWXYZ
-Protein , 5 types, 5 molecules 34567
| #3: Protein | Mass: 22395.326 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NWT8 |
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| #4: Protein | Mass: 78648.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EY7 |
| #5: Protein | Mass: 39600.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: Q8WVM0, Transferases; Transferring one-carbon groups; Methyltransferases |
| #6: Protein | Mass: 38417.434 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N0V3 |
| #7: Protein | Mass: 50807.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: Q9H7H0, Transferases; Transferring one-carbon groups; Methyltransferases |
-RNA chain , 1 types, 1 molecules A
| #8: RNA chain | Mass: 306449.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1858624182 |
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-Non-polymers , 9 types, 39 molecules 
















| #34: Chemical | ChemComp-SF4 / | ||||||||||||
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| #35: Chemical | ChemComp-SAM / | ||||||||||||
| #36: Chemical | ChemComp-K / #37: Chemical | ChemComp-MG / #38: Chemical | ChemComp-NAD / | #39: Chemical | ChemComp-ZN / | #40: Chemical | #41: Chemical | ChemComp-ATP / | #42: Chemical | ChemComp-GDP / | |
-Details
| Has ligand of interest | 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 mitochondrial small subunit assembly intermediate, State C* Type: RIBOSOME / Entity ID: #1-#33 / Source: NATURAL |
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| Molecular weight | Value: 1 MDa / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: FEI VITROBOT MARK IV / 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 magnification: 64000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 700 nm |
| Specimen holder | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 51 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 47037 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 9109335 | ||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 33642 Details: 11 focused maps calculated in RELION 3.1.1 were combined into a composite map using phenix.combine_focused_maps. Composite half maps were generated by combining each half map from focused refinements. Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Space: REAL | ||||||||||||||||||||||||||||||||||||||||
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About Yorodumi



Homo sapiens (human)
United States, 2items
Citation
















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