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Yorodumi- PDB-7nqh: 55S mammalian mitochondrial ribosome with mtRF1a and P-site tRNAMet -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7nqh | |||||||||
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| Title | 55S mammalian mitochondrial ribosome with mtRF1a and P-site tRNAMet | |||||||||
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Keywords | TRANSLATION / Ribosome / Mitochondria / Termination / mtRF1a / Release | |||||||||
| Function / homology | Function and homology informationHormone ligand-binding receptors / G alpha (q) signalling events / gonadotropin hormone-releasing hormone activity / gonadotropin-releasing hormone receptor binding / Mitochondrial translation elongation / Mitochondrial translation termination / mitochondrial translational termination / mitochondrial transcription / mitochondrial ribosome assembly / translation release factor activity, codon specific ...Hormone ligand-binding receptors / G alpha (q) signalling events / gonadotropin hormone-releasing hormone activity / gonadotropin-releasing hormone receptor binding / Mitochondrial translation elongation / Mitochondrial translation termination / mitochondrial translational termination / mitochondrial transcription / mitochondrial ribosome assembly / translation release factor activity, codon specific / mitochondrial translational elongation / ribonuclease III activity / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial protein degradation / translation release factor activity / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / mitochondrial translation / organelle membrane / apoptotic mitochondrial changes / positive regulation of proteolysis / ribosomal small subunit binding / RNA processing / rescue of stalled ribosome / cell junction / large ribosomal subunit / double-stranded RNA binding / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / nuclear membrane / negative regulation of translation / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / intracellular membrane-bounded organelle / mRNA binding / positive regulation of DNA-templated transcription / nucleolus / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human)![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Kummer, E. / Schubert, K. / Ban, N. | |||||||||
| Funding support | Switzerland, 2items
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Citation | Journal: Mol Cell / Year: 2021Title: Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. Authors: Eva Kummer / Katharina Noel Schubert / Tanja Schoenhut / Alain Scaiola / Nenad Ban / ![]() Abstract: The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as ...The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as a screening tool to identify mitochondrial translation termination mechanisms and to describe them in molecular detail. We show how mitochondrial release factor 1a releases the nascent chain from the ribosome when it encounters the canonical stop codons UAA and UAG. Furthermore, we define how the peptidyl-tRNA hydrolase ICT1 acts as a rescue factor on mitoribosomes that have stalled on truncated messages to recover them for protein synthesis. Finally, we present structural models detailing the process of mitochondrial ribosome recycling to explain how a dedicated elongation factor, mitochondrial EFG2 (mtEFG2), has specialized for cooperation with the mitochondrial ribosome recycling factor to dissociate the mitoribosomal subunits at the end of the translation process. | |||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7nqh.cif.gz | 3.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7nqh.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7nqh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7nqh_validation.pdf.gz | 2.4 MB | Display | wwPDB validaton report |
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| Full document | 7nqh_full_validation.pdf.gz | 2.5 MB | Display | |
| Data in XML | 7nqh_validation.xml.gz | 370.5 KB | Display | |
| Data in CIF | 7nqh_validation.cif.gz | 619.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nq/7nqh ftp://data.pdbj.org/pub/pdb/validation_reports/nq/7nqh | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 12527MC ![]() 7nqlC ![]() 7nshC ![]() 7nsiC ![]() 7nsjC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
+Mitochondrial ribosomal protein ... , 38 types, 43 molecules CLDLELFLGLHLB0B1B2BFBIBJBKBSBTBUBVBaBbBcBeBgBiBjBmBnBtBxB7AB...
-RNA chain , 5 types, 5 molecules BBAAAVAXBA
| #5: RNA chain | Mass: 23402.018 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #48: RNA chain | Mass: 308989.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #68: RNA chain | Mass: 22664.498 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: GenBank: 1208989970 |
| #69: RNA chain | Mass: 2839.767 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
| #88: RNA chain | Mass: 504852.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Protein , 39 types, 39 molecules BDBEBLBNBOBPBQBRBWBXBYB3BdBfBhBlBoBpBqBuBvB4B5B6AFAIAKAOAQAU...
-39S ribosomal protein ... , 2 types, 2 molecules BkBw
| #36: Protein | Mass: 29942.523 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #46: Protein | Mass: 49100.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-28S ribosomal protein ... , 3 types, 3 molecules AGAPAp
| #57: Protein | Mass: 27778.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #64: Protein | Mass: 15182.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #86: Protein | Mass: 29220.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide , 1 types, 1 molecules AZ
| #70: Protein/peptide | Mass: 1549.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: unknown polypeptide modeled as poly-Alanine / Source: (natural) ![]() |
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-Non-polymers , 6 types, 338 molecules 










| #89: Chemical | ChemComp-MG / #90: Chemical | ChemComp-ZN / #91: Chemical | #92: Chemical | ChemComp-GTP / | #93: Chemical | #94: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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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
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| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 7.6 | ||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE-PROPANE |
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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 |
| 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
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 47048 / Symmetry type: POINT |
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Homo sapiens (human)

Switzerland, 2items
Citation
UCSF Chimera


















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