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Yorodumi- PDB-8csq: Human mitochondrial small subunit assembly intermediate (State B) -
+Open data
-Basic information
Entry | Database: PDB / ID: 8csq | |||||||||
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Title | Human mitochondrial small subunit assembly intermediate (State B) | |||||||||
Components |
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Keywords | RIBOSOME / Ribonucleoprotein complex / Mitochondria Biogenesis | |||||||||
Function / homology | Function and homology information mitochondrial small ribosomal subunit assembly / rRNA modification in the mitochondrion / mitochondrial transcription factor activity / transcription initiation at mitochondrial promoter / rRNA modification / rRNA (adenine-N6,N6-)-dimethyltransferase activity / Mitochondrial Fatty Acid Beta-Oxidation / mitochondrial ribosome binding / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity ...mitochondrial small ribosomal subunit assembly / rRNA modification in the mitochondrion / mitochondrial transcription factor activity / transcription initiation at mitochondrial promoter / rRNA modification / rRNA (adenine-N6,N6-)-dimethyltransferase activity / Mitochondrial Fatty Acid Beta-Oxidation / mitochondrial ribosome binding / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / positive regulation of mitochondrial translation / Mitochondrial translation initiation / S-adenosyl-L-methionine binding / negative regulation of mitotic nuclear division / mitochondrial ribosome / mitochondrial small ribosomal subunit / rRNA methylation / mitochondrial translation / fatty acid beta-oxidation / 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 / fatty acid biosynthetic process / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / cell junction / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 4 iron, 4 sulfur cluster binding / nuclear membrane / cell population proliferation / tRNA binding / mitochondrial inner membrane / rRNA binding / ribosome / structural constituent of ribosome / mitochondrial matrix / translation / protein domain specific binding / intracellular membrane-bounded organelle / mRNA binding / nucleolus / GTP binding / mitochondrion / DNA binding / RNA binding / nucleoplasm / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.54 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 viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8csq.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8csq.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 8csq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8csq_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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Full document | 8csq_full_validation.pdf.gz | 1.9 MB | Display | |
Data in XML | 8csq_validation.xml.gz | 173.1 KB | Display | |
Data in CIF | 8csq_validation.cif.gz | 280.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/8csq ftp://data.pdbj.org/pub/pdb/validation_reports/cs/8csq | HTTPS FTP |
-Related structure data
Related structure data | 26967MC 8cspC 8csrC 8cssC 8cstC 8csuC 8d8jC 8d8kC 8d8lC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
+28S ribosomal protein ... , 26 types, 26 molecules 01BCDEFGHJKLMNOPQRSTUVWXYZ
-Protein , 6 types, 6 molecules 34578a
#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: 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 |
#7: Protein | Mass: 43019.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: Q8IVS2, [acyl-carrier-protein] S-malonyltransferase |
#33: Protein | Mass: 48413.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75616 |
-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 , 8 types, 38 molecules
#34: Chemical | ChemComp-SF4 / | ||||||||||
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#35: Chemical | ChemComp-SAM / | ||||||||||
#36: Chemical | ChemComp-K / #37: Chemical | ChemComp-MG / #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
Component | Name: Human mitochondrial small subunit assembly intermediate, State B 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 |
-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
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 9109335 | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.54 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 203950 Details: 12 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 | 3D fitting-ID: 1 / Source name: PDB / Type: experimental model
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