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Yorodumi- PDB-7l20: Cryo-EM structure of the human 39S mitoribosomal subunit in compl... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7l20 | ||||||
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| Title | Cryo-EM structure of the human 39S mitoribosomal subunit in complex with RRFmt and EF-G2mt. | ||||||
Components |
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Keywords | RIBOSOME / Cryo-EM / Mammalian / mito-ribosome / mtEFg2 / mtRRF | ||||||
| Function / homology | Function and homology informationmitochondrial translational termination / mitochondrial transcription / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase ...mitochondrial translational termination / mitochondrial transcription / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / mitochondrial small ribosomal subunit / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / ribosome disassembly / peptidyl-tRNA hydrolase activity / mitochondrial translation / ribosomal large subunit binding / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled ribosome / cellular response to leukemia inhibitory factor / fibrillar center / cell junction / double-stranded RNA binding / large ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / mitochondrial inner 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 / GTPase activity / mRNA binding / apoptotic process / positive regulation of DNA-templated transcription / GTP binding / nucleolus / mitochondrion / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.15 Å | ||||||
Authors | Agrawal, E. / Koripella, R. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2021Title: Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance. Authors: Ravi Kiran Koripella / Ayush Deep / Ekansh K Agrawal / Pooja Keshavan / Nilesh K Banavali / Rajendra K Agrawal / ![]() Abstract: Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we ...Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF) and a recycling-specific homolog of elongation factor G (EF-G2). These structures clarify an unusual role of a mitochondria-specific segment of RRF, identify the structural distinctions that confer functional specificity to EF-G2, and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling. Furthermore, biochemical and structural analyses reveal that the molecular mechanism of antibiotic fusidic acid resistance for EF-G2 is markedly different from that of mitochondrial elongation factor EF-G1, suggesting that the two human EF-Gs have evolved diversely to negate the effect of a bacterial antibiotic. | ||||||
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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 | 7l20.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7l20.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7l20.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7l20_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 7l20_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 7l20_validation.xml.gz | 227.1 KB | Display | |
| Data in CIF | 7l20_validation.cif.gz | 392.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l2/7l20 ftp://data.pdbj.org/pub/pdb/validation_reports/l2/7l20 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 23121MC ![]() 7l08C M: map data used to model this data C: citing same article ( |
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| Similar structure data | |
| EM raw data | EMPIAR-10703 (Title: Distinct mechanisms of the human mitoribosome recycling and antibiotic resistanceData size: 2.3 TB Data #1: Aligned single-frame particles of human mitochondrial 55S-EF-Gmt complex [picked particles - single frame - processed]) |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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Components
-RNA chain , 2 types, 2 molecules AB
| #1: RNA chain | Mass: 500019.594 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1563835895 |
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| #2: RNA chain | Mass: 23266.883 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
+39S ribosomal protein ... , 46 types, 48 molecules DFHKLMORSTWXYZ012348begimrJINU...
-Protein , 8 types, 8 molecules joqPpuzw
| #27: Protein | Mass: 13696.684 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: A8K7J6 |
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| #29: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BQC6 |
| #30: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8TAE8 |
| #35: Protein | Mass: 20465.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: A8K9D2 |
| #50: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q14197, peptidyl-tRNA hydrolase |
| #53: Protein | Mass: 5549.833 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #55: Protein | Mass: 22590.197 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96E11 |
| #56: Protein | Mass: 77306.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q969S9 |
-Non-polymers , 3 types, 106 molecules 




| #57: Chemical | ChemComp-MG / #58: Chemical | #59: Chemical | ChemComp-GCP / | |
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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
| Component | Name: Cryo-EM structure of Mammalian Mitochondrial ribosome complex with mtEFG-2 and mtRRF Type: RIBOSOME Details: Cryo-EM structure of Mammalian Mitochondrial ribosome complex with mtEFG-2 and mtRRF-Class-3 Entity ID: #1-#56 / Source: NATURAL |
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| 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 | Cryogen name: ETHANE |
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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: OTHER / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: OTHER |
| Image recording | Electron dose: 71 e/Å2 / Film or detector model: DIRECT ELECTRON DE-16 (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.15 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 132008 / Symmetry type: POINT |
| Atomic model building | Protocol: OTHER |
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About Yorodumi



Homo sapiens (human)
United States, 1items
Citation
UCSF Chimera













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