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Yorodumi- PDB-6ydp: 55S mammalian mitochondrial ribosome with mtEFG1 and P site fMet-... -
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Basic information
| Entry | Database: PDB / ID: 6ydp | ||||||||||||
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| Title | 55S mammalian mitochondrial ribosome with mtEFG1 and P site fMet-tRNAMet (POST) | ||||||||||||
Components |
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Keywords | TRANSLATION / Mitochondria / 55S ribosome / mtEFG1 / Elongation | ||||||||||||
| 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 / mitochondrial translational elongation ...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 / mitochondrial translational elongation / ribonuclease III activity / Mitochondrial translation elongation / translation release factor activity, codon nonspecific / Mitochondrial protein degradation / 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 / translation elongation factor activity / RNA processing / rescue of stalled ribosome / cell junction / regulation of translation / double-stranded RNA binding / large ribosomal subunit / 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 / negative regulation of translation / mitochondrial inner membrane / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / GTPase activity / mRNA binding / positive regulation of DNA-templated transcription / GTP binding / 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 Å | ||||||||||||
Authors | Kummer, E. / Ban, N. | ||||||||||||
| Funding support | Switzerland, 3items
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Citation | Journal: EMBO J / Year: 2020Title: Structural insights into mammalian mitochondrial translation elongation catalyzed by mtEFG1. Authors: Eva Kummer / Nenad Ban / ![]() Abstract: Mitochondria are eukaryotic organelles of bacterial origin where respiration takes place to produce cellular chemical energy. These reactions are catalyzed by the respiratory chain complexes located ...Mitochondria are eukaryotic organelles of bacterial origin where respiration takes place to produce cellular chemical energy. These reactions are catalyzed by the respiratory chain complexes located in the inner mitochondrial membrane. Notably, key components of the respiratory chain complexes are encoded on the mitochondrial chromosome and their expression relies on a dedicated mitochondrial translation machinery. Defects in the mitochondrial gene expression machinery lead to a variety of diseases in humans mostly affecting tissues with high energy demand such as the nervous system, the heart, or the muscles. The mitochondrial translation system has substantially diverged from its bacterial ancestor, including alterations in the mitoribosomal architecture, multiple changes to the set of translation factors and striking reductions in otherwise conserved tRNA elements. Although a number of structures of mitochondrial ribosomes from different species have been determined, our mechanistic understanding of the mitochondrial translation cycle remains largely unexplored. Here, we present two cryo-EM reconstructions of human mitochondrial elongation factor G1 bound to the mammalian mitochondrial ribosome at two different steps of the tRNA translocation reaction during translation elongation. Our structures explain the mechanism of tRNA and mRNA translocation on the mitoribosome, the regulation of mtEFG1 activity by the ribosomal GTPase-associated center, and the basis of decreased susceptibility of mtEFG1 to the commonly used antibiotic fusidic acid. | ||||||||||||
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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 | 6ydp.cif.gz | 4.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb6ydp.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 6ydp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6ydp_validation.pdf.gz | 2.5 MB | Display | wwPDB validaton report |
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| Full document | 6ydp_full_validation.pdf.gz | 2.6 MB | Display | |
| Data in XML | 6ydp_validation.xml.gz | 374.4 KB | Display | |
| Data in CIF | 6ydp_validation.cif.gz | 622 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yd/6ydp ftp://data.pdbj.org/pub/pdb/validation_reports/yd/6ydp | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 10778MC ![]() 6ydwC 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 ... , 39 types, 45 molecules B0BUBVBaBbBcBeBgBiBjBmBnBtB1BxABACAEAGAJALANARAaAcAdAeB2AhAk...
+Protein , 37 types, 37 molecules BWBXBYBfBhBlBoBpBqBuBvAFAIAKAOAQAUAbAfAgAiAjAmAnAoB3B4B5B6B9...
-Uncharacterized ... , 2 types, 2 molecules BdBR
| #10: Protein | Mass: 24075.658 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #85: Protein | Mass: 19268.178 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-39S ribosomal protein ... , 2 types, 2 molecules BkBw
| #17: Protein | Mass: 29942.523 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #27: Protein | Mass: 49100.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA chain , 4 types, 5 molecules AABAAVAXBB
| #30: RNA chain | Mass: 5350865.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #46: RNA chain | | Mass: 22664.498 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: GenBank: 1208989970#47: RNA chain | | Mass: 1892.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)#73: RNA chain | | Mass: 23402.018 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-28S ribosomal protein ... , 2 types, 2 molecules APAp
| #42: Protein | Mass: 15182.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #64: 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
| #48: Protein/peptide | Mass: 1297.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 8 types, 345 molecules 














| #88: Chemical | ChemComp-MG / #89: Chemical | ChemComp-ZN / #90: Chemical | #91: Chemical | ChemComp-FME / | #92: Chemical | ChemComp-GTP / | #93: Chemical | #94: Chemical | ChemComp-GNP / | #95: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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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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| Buffer solution | pH: 7.6 | ||||||||||||||||||||||||||||||
| Specimen | Conc.: 0.017 mg/ml / 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: OTHER |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| EM software | Name: EPU / Version: 1.9.0.30REL / Category: image acquisition |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| Symmetry | Point symmetry: C1 (asymmetric) |
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 97764 / Symmetry type: POINT |
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |
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Homo sapiens (human)

Switzerland, 3items
Citation
UCSF Chimera












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