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- PDB-7pnt: Assembly intermediate of mouse mitochondrial ribosome small subun... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7pnt | ||||||||||||
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Title | Assembly intermediate of mouse mitochondrial ribosome small subunit without mS37 in complex with RbfA and Tfb1m | ||||||||||||
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![]() | RIBOSOME / Assembly intermediate / maturation / biogenesis / small subunit / mitochondrion | ||||||||||||
Function / homology | ![]() Mitochondrial translation elongation / Mitochondrial translation termination / mitochondrial transcription factor activity / transcription initiation at mitochondrial promoter / rRNA (adenine-N6,N6-)-dimethyltransferase activity / mitochondrial ribosome binding / anaphase-promoting complex / Mitochondrial protein degradation / mitochondrial ribosome assembly / positive regulation of mitochondrial translation ...Mitochondrial translation elongation / Mitochondrial translation termination / mitochondrial transcription factor activity / transcription initiation at mitochondrial promoter / rRNA (adenine-N6,N6-)-dimethyltransferase activity / mitochondrial ribosome binding / anaphase-promoting complex / Mitochondrial protein degradation / mitochondrial ribosome assembly / positive regulation of mitochondrial translation / S-adenosyl-L-methionine binding / mitochondrial small ribosomal subunit / rRNA methylation / mitochondrial ribosome / mitochondrial translation / mitochondrial nucleoid / apoptotic mitochondrial changes / positive regulation of proteolysis / ribosomal small subunit binding / Transferases; Transferring one-carbon groups; Methyltransferases / rRNA processing / cell junction / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit rRNA binding / nuclear membrane / cell population proliferation / mitochondrial inner membrane / tRNA binding / rRNA binding / ribosome / protein ubiquitination / structural constituent of ribosome / mitochondrial matrix / translation / protein domain specific binding / mRNA binding / nucleolus / mitochondrion / DNA binding / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.19 Å | ||||||||||||
![]() | Itoh, Y. / Khawaja, A. / Laptev, I. / Sergiev, P. / Rorbach, J. / Amunts, A. | ||||||||||||
Funding support | European Union, 3items
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![]() | ![]() Title: Mechanism of mitoribosomal small subunit biogenesis and preinitiation. Authors: Yuzuru Itoh / Anas Khawaja / Ivan Laptev / Miriam Cipullo / Ilian Atanassov / Petr Sergiev / Joanna Rorbach / Alexey Amunts / ![]() ![]() ![]() Abstract: Mitoribosomes are essential for the synthesis and maintenance of bioenergetic proteins. Here we use cryo-electron microscopy to determine a series of the small mitoribosomal subunit (SSU) ...Mitoribosomes are essential for the synthesis and maintenance of bioenergetic proteins. Here we use cryo-electron microscopy to determine a series of the small mitoribosomal subunit (SSU) intermediates in complex with auxiliary factors, revealing a sequential assembly mechanism. The methyltransferase TFB1M binds to partially unfolded rRNA h45 that is promoted by RBFA, while the mRNA channel is blocked. This enables binding of METTL15 that promotes further rRNA maturation and a large conformational change of RBFA. The new conformation allows initiation factor mtIF3 to already occupy the subunit interface during the assembly. Finally, the mitochondria-specific ribosomal protein mS37 (ref. ) outcompetes RBFA to complete the assembly with the SSU-mS37-mtIF3 complex that proceeds towards mtIF2 binding and translation initiation. Our results explain how the action of step-specific factors modulate the dynamic assembly of the SSU, and adaptation of a unique protein, mS37, links the assembly to initiation to establish the catalytic human mitoribosome. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.6 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 13551MC ![]() 7pnuC ![]() 7pnvC ![]() 7pnwC ![]() 7pnxC ![]() 7pnyC ![]() 7pnzC ![]() 7po0C ![]() 7po1C ![]() 7po2C ![]() 7po3C ![]() 7po4C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-RNA chain , 1 types, 1 molecules A
#1: RNA chain | Mass: 306793.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() ![]() |
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+28S ribosomal protein ... , 27 types, 27 molecules BCDEFGHIJKLMNOPQRSTUVWXYZ01
-Protein , 4 types, 4 molecules 34ac
#29: Protein | Mass: 23345.412 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() ![]() |
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#30: Protein | Mass: 77890.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() ![]() |
#31: Protein | Mass: 39382.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() ![]() |
#32: Protein | Mass: 39019.602 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() ![]() References: UniProt: Q8JZM0, Transferases; Transferring one-carbon groups; Methyltransferases |
-Non-polymers , 6 types, 515 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/K.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/K.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/HOH.gif)
#33: Chemical | ChemComp-MG / #34: Chemical | ChemComp-K / #35: Chemical | ChemComp-ZN / | #36: Chemical | #37: Chemical | ChemComp-ATP / | #38: Water | ChemComp-HOH / | |
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-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: Assembly intermediate of small subunit of human mitochondrial ribosome Type: RIBOSOME / Entity ID: #1-#32 / Source: NATURAL | ||||||||||||||||||||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
Source (natural) | Organism: ![]() ![]() | ||||||||||||||||||||||||||||||
Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1 | ||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 297 K |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 165000 X / Nominal defocus max: 3600 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 4 sec. / Electron dose: 31 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 26468 |
EM imaging optics | Energyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV |
Image scans | Movie frames/image: 20 / Used frames/image: 1-20 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 3076615 | ||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.19 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 52361 / Algorithm: BACK PROJECTION / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Space: REAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 6RW4 Accession code: 6RW4 / Source name: PDB / Type: experimental model |