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Yorodumi- PDB-6nu2: Structural insights into unique features of the human mitochondri... -
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Basic information
| Entry | Database: PDB / ID: 6nu2 | |||||||||
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| Title | Structural insights into unique features of the human mitochondrial ribosome recycling | |||||||||
|  Components | 
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|  Keywords | RIBOSOME / mitochondrial ribosome recycling Factor / mtRRF / 55S | |||||||||
| Function / homology |  Function and homology information rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial ribosome assembly / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / negative regulation of mitotic nuclear division ...rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial ribosome assembly / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / negative regulation of mitotic nuclear division / 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 / apoptotic mitochondrial changes / ribosomal large subunit binding / positive regulation of proteolysis / ribosomal small subunit binding / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled ribosome / cellular response to leukemia inhibitory factor / apoptotic signaling pathway / fibrillar center / cell junction / double-stranded RNA binding / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / nuclear membrane / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / tRNA binding / cell population proliferation / 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 / intracellular membrane-bounded organelle / mRNA binding / apoptotic process / 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: 3.9 Å | |||||||||
|  Authors | Sharma, M.R. / Koripella, R.K. / Agrawal, R.K. | |||||||||
| Funding support |  United States, 2items 
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|  Citation |  Journal: Proc Natl Acad Sci U S A / Year: 2019 Title: Structural insights into unique features of the human mitochondrial ribosome recycling. Authors: Ravi K Koripella / Manjuli R Sharma / Paul Risteff / Pooja Keshavan / Rajendra K Agrawal /  Abstract: Mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with ...Mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with bacteria, the composition and structure of the human mitoribosome and its translational factors are significantly different from those of their bacterial counterparts. The mammalian mitoribosome recycling factor (RRF) carries a mito-specific N terminus extension (NTE), which is necessary for the function of RRF Here we present a 3.9-Å resolution cryo-electron microscopic (cryo-EM) structure of the human 55S mitoribosome-RRF complex, which reveals α-helix and loop structures for the NTE that makes multiple mito-specific interactions with functionally critical regions of the mitoribosome. These include ribosomal RNA segments that constitute the peptidyl transferase center (PTC) and those that connect PTC with the GTPase-associated center and with mitoribosomal proteins L16 and L27. Our structure reveals the presence of a tRNA in the pe/E position and a rotation of the small mitoribosomal subunit on RRF binding. In addition, we observe an interaction between the pe/E tRNA and a mito-specific protein, mL64. These findings help understand the unique features of mitoribosome recycling. | |||||||||
| History | 
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- Structure visualization
Structure visualization
| Movie | 
 
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| Structure viewer | Molecule:  Molmil  Jmol/JSmol | 
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| PDBx/mmCIF format |  6nu2.cif.gz | 6 MB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb6nu2.ent.gz | Display |  PDB format | |
| PDBx/mmJSON format |  6nu2.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  6nu2_validation.pdf.gz | 1.3 MB | Display |  wwPDB validaton report | 
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| Full document |  6nu2_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML |  6nu2_validation.xml.gz | 306.6 KB | Display | |
| Data in CIF |  6nu2_validation.cif.gz | 528.9 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/nu/6nu2  ftp://data.pdbj.org/pub/pdb/validation_reports/nu/6nu2 | HTTPS FTP | 
-Related structure data
| Related structure data |  0514MC  0515C  6nu3C M: map data used to model this data C: citing same article ( | 
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| Similar structure data | 
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- Assembly
Assembly
| Deposited unit |  
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| 1 | 
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- Components
Components
-RNA chain , 4 types, 4 molecules ABuAA   
| #1: RNA chain | Mass: 472442.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
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| #2: RNA chain | Mass: 17955.715 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
| #54: RNA chain | Mass: 589.430 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
| #56: RNA chain | Mass: 296318.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
+39S ribosomal protein  ... , 47 types, 47 molecules DEFHIJKLMNOPQRSTUVWXYZ01234567...                              
-Protein , 7 types, 7 molecules opqzA2A3A4      
| #48: Protein | Mass: 11316.099 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q9BQC6 | 
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| #49: Protein | Mass: 18024.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q14197, peptidyl-tRNA hydrolase | 
| #50: Protein | Mass: 15301.280 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q8TAE8 | 
| #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 | 
| #84: Protein | Mass: 13280.546 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q96BP2 | 
| #85: Protein | Mass: 8722.630 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q9NWT8 | 
| #86: Protein | Mass: 50095.523 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q96EY7 | 
-Protein/peptide , 1 types, 1 molecules t
| #53: Protein/peptide | Mass: 2400.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
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+28S ribosomal protein  ... , 27 types, 27 molecules ABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAVAWAXAYAZA0A1                          
-Non-polymers , 2 types, 134 molecules 


| #87: Chemical | ChemComp-MG / #88: Chemical | ChemComp-ZN / | 
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-Details
| Has protein modification | 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
Sample preparation
| Component | Name: Structural insights into unique features of the human mitochondrial ribosome bound with mtRRF -Class-1 Type: RIBOSOME Details: Structure of human mitochondrial ribosome complex with mtRRF -Class-1 Entity ID: #1-#86 / Source: NATURAL | 
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| Source (natural) | Organism:  Homo sapiens (human) | 
| Buffer solution | pH: 7.6 | 
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | 
| Specimen support | Details: unspecified | 
| Vitrification | Cryogen name: ETHANE | 
- Electron microscopy imaging
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: 70 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) | 
- Processing
Processing
| EM software | 
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| CTF correction | Type: NONE | ||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 67116 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| Atomic model building | B value: 97 / Protocol: OTHER | ||||||||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 3JD5 Accession code: 3JD5 / Source name: PDB / Type: experimental model | 
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