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Yorodumi- PDB-8cst: Human mitochondrial small subunit assembly intermediate (State E) -
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Open data
- Basic information
Basic information
| Entry | Database: PDB / ID: 8cst | |||||||||
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| Title | Human mitochondrial small subunit assembly intermediate (State E) | |||||||||
|  Components | 
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|  Keywords | RIBOSOME / Ribonucleoprotein complex Mitochondria Biogenesis | |||||||||
| Function / homology |  Function and homology information mitochondrial small ribosomal subunit assembly / mitochondrial ribosome binding / 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 ...mitochondrial small ribosomal subunit assembly / mitochondrial ribosome binding / 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 / mitochondrial translation / apoptotic mitochondrial changes / positive regulation of proteolysis / ribosomal small subunit binding / Mitochondrial protein degradation / apoptotic signaling pathway / 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 / 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: 2.85 Å | |||||||||
|  Authors | Harper, N.J. / Burnside, C. / Klinge, S. | |||||||||
| Funding support |  United States, 2items 
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|  Citation |  Journal: Nature / Year: 2023 Title: 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. | |||||||||
| History | 
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- Structure visualization
Structure visualization
| Structure viewer | Molecule:  Molmil  Jmol/JSmol | 
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- Downloads & links
Downloads & links
- Download
Download
| PDBx/mmCIF format |  8cst.cif.gz | 1.5 MB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb8cst.ent.gz | 1.2 MB | Display |  PDB format | 
| PDBx/mmJSON format |  8cst.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  8cst_validation.pdf.gz | 1.9 MB | Display |  wwPDB validaton report | 
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| Full document |  8cst_full_validation.pdf.gz | 1.9 MB | Display | |
| Data in XML |  8cst_validation.xml.gz | 167.5 KB | Display | |
| Data in CIF |  8cst_validation.cif.gz | 269.7 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/cs/8cst  ftp://data.pdbj.org/pub/pdb/validation_reports/cs/8cst | HTTPS FTP | 
-Related structure data
| Related structure data |  26970MC  8cspC  8csqC  8csrC  8cssC  8csuC  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 | 
- Links
Links
- Assembly
Assembly
| Deposited unit |  
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| 1 | 
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- Components
Components
+28S ribosomal protein  ... , 27 types, 27 molecules 01BCDEFGHIJKLMNOPQRSTUVWXYZ                          
-Protein , 4 types, 4 molecules 3467   
| #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: 38417.434 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q8N0V3 | 
| #6: 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
| #7: RNA chain | Mass: 306505.438 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, 42 molecules 
















| #33: Chemical | ChemComp-SF4 / | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| #34: Chemical | ChemComp-SAM / | ||||||||||||
| #35: Chemical | ChemComp-K / #36: Chemical | ChemComp-MG / #37: Chemical | ChemComp-NAD / | #38: Chemical | ChemComp-ZN / | #39: Chemical | #40: Chemical | ChemComp-ATP / | #41: 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 | 
- Sample preparation
Sample preparation
| Component | Name: Human mitochondrial small subunit assembly intermediate, State E Type: RIBOSOME / Entity ID: #1-#32 / 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 | 
- Electron microscopy imaging
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 | 
- Processing
Processing
| EM software | 
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 9109335 | ||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 39864 Details: 10 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 | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | 
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