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Yorodumi- PDB-8any: Human mitochondrial ribosome in complex with LRPPRC, SLIRP, A-sit... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8any | ||||||||||||||||||
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| Title | Human mitochondrial ribosome in complex with LRPPRC, SLIRP, A-site, P-site, E-site tRNAs and mRNA | ||||||||||||||||||
Components |
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Keywords | RIBOSOME / mitochondrial translation / mRNA delivery | ||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of mitochondrial RNA catabolic process / Mitochondrial RNA degradation / mitochondrial RNA catabolic process / regulation of mitochondrial translation / rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial transcription / mitochondrial ribosome assembly / mitochondrial translational elongation / Mitochondrial translation elongation ...negative regulation of mitochondrial RNA catabolic process / Mitochondrial RNA degradation / mitochondrial RNA catabolic process / regulation of mitochondrial translation / rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial transcription / mitochondrial ribosome assembly / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / flagellated sperm motility / translation release factor activity / negative regulation of mitotic nuclear division / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / mitochondrial small ribosomal subunit / nuclear inner membrane / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / peptidyl-tRNA hydrolase activity / mitochondrial translation / mitochondrion transport along microtubule / apoptotic mitochondrial changes / nuclear outer membrane / positive regulation of proteolysis / mitochondrial nucleoid / ribosomal small subunit binding / anatomical structure morphogenesis / spermatid development / mRNA transport / single fertilization / sperm flagellum / RNA processing / beta-tubulin binding / rescue of stalled ribosome / acrosomal vesicle / Mitochondrial protein degradation / cellular response to leukemia inhibitory factor / mRNA 3'-UTR binding / condensed nuclear chromosome / mitochondrion organization / apoptotic signaling pathway / autophagy / fibrillar center / cell junction / single-stranded DNA binding / regulation of translation / double-stranded RNA binding / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / nuclear membrane / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cytoskeleton / tRNA binding / cell population proliferation / 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 / intracellular membrane-bounded organelle / mRNA binding / apoptotic process / ubiquitin protein ligase binding / positive regulation of DNA-templated transcription / GTP binding / nucleolus / perinuclear region of cytoplasm / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.85 Å | ||||||||||||||||||
Authors | Singh, V. / Itoh, Y. / Amunts, A. | ||||||||||||||||||
| Funding support | Sweden, European Union, 5items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024Title: Structural basis of LRPPRC-SLIRP-dependent translation by the mitoribosome. Authors: Vivek Singh / J Conor Moran / Yuzuru Itoh / Iliana C Soto / Flavia Fontanesi / Mary Couvillion / Martijn A Huynen / L Stirling Churchman / Antoni Barrientos / Alexey Amunts / ![]() Abstract: In mammalian mitochondria, mRNAs are cotranscriptionally stabilized by the protein factor LRPPRC (leucine-rich pentatricopeptide repeat-containing protein). Here, we characterize LRPPRC as an mRNA ...In mammalian mitochondria, mRNAs are cotranscriptionally stabilized by the protein factor LRPPRC (leucine-rich pentatricopeptide repeat-containing protein). Here, we characterize LRPPRC as an mRNA delivery factor and report its cryo-electron microscopy structure in complex with SLIRP (SRA stem-loop-interacting RNA-binding protein), mRNA and the mitoribosome. The structure shows that LRPPRC associates with the mitoribosomal proteins mS39 and the N terminus of mS31 through recognition of the LRPPRC helical repeats. Together, the proteins form a corridor for handoff of the mRNA. The mRNA is directly bound to SLIRP, which also has a stabilizing function for LRPPRC. To delineate the effect of LRPPRC on individual mitochondrial transcripts, we used RNA sequencing, metabolic labeling and mitoribosome profiling, which showed a transcript-specific influence on mRNA translation efficiency, with cytochrome c oxidase subunit 1 and 2 translation being the most affected. Our data suggest that LRPPRC-SLIRP acts in recruitment of mitochondrial mRNAs to modulate their translation. Collectively, the data define LRPPRC-SLIRP as a regulator of the mitochondrial gene expression system. | ||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8any.cif.gz | 7.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8any.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8any.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/8any ftp://data.pdbj.org/pub/pdb/validation_reports/an/8any | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 15544MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 7 types, 7 molecules AAAwAxAyABAz
| #1: RNA chain | Mass: 306218.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: GenBank: 1858621102 |
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| #30: RNA chain | Mass: 21627.838 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) |
| #31: RNA chain | Mass: 22354.291 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) |
| #32: RNA chain | Mass: 22369.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) |
| #33: RNA chain | Mass: 500727.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) |
| #34: RNA chain | Mass: 22989.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) |
| #91: RNA chain | Mass: 13286.822 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) |
+28S ribosomal protein ... , 27 types, 27 molecules ABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAVAWAXAZA0A1AY
-Protein , 9 types, 9 molecules A2A3bopqA5A4A6
| #28: Protein | Mass: 13540.856 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q96BP2 |
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| #29: Protein | Mass: 22395.326 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NWT8 |
| #67: Protein | Mass: 23352.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N983 |
| #79: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BQC6 |
| #80: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q14197, peptidyl-tRNA hydrolase |
| #81: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q8TAE8 |
| #88: Protein | Mass: 158098.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: P42704 |
| #89: Protein | Mass: 78648.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EY7 |
| #90: Protein | Mass: 12371.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) Homo sapiens (human) / References: UniProt: Q9GZT3 |
+39S ribosomal protein ... , 48 types, 53 molecules DEFIJKLMNOPQRSTUVWXYZ012345678...
-Non-polymers , 12 types, 7197 molecules 






















| #92: Chemical | ChemComp-NAD / | ||||||||||||||||||
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| #93: Chemical | ChemComp-SPM / | ||||||||||||||||||
| #94: Chemical | ChemComp-SPD / #95: Chemical | ChemComp-MG / #96: Chemical | ChemComp-K / #97: Chemical | #98: Chemical | #99: Chemical | ChemComp-ATP / | #100: Chemical | ChemComp-GDP / | #101: Chemical | ChemComp-PUT / | #102: Chemical | ChemComp-VAL / | #103: Water | ChemComp-HOH / | |
-Details
| Has ligand of interest | N |
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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: Human mitochondrial ribosome bound to LRPPRC-SLIRP, mRNA and tRNAs in the A-site, P-site and E-site Type: RIBOSOME / Entity ID: #1-#33, #35-#66, #68-#91 / 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2800 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 30 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| EM imaging optics | Energyfilter slit width: 20 eV |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 82522 / Symmetry type: POINT |
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Homo sapiens (human)
Sweden, European Union, 5items
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FIELD EMISSION GUN