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- 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 | ||||||||||||||||||
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![]() | RIBOSOME / mitochondrial translation / mRNA delivery | ||||||||||||||||||
Function / homology | ![]() negative regulation of mitochondrial RNA catabolic process / Mitochondrial RNA degradation / mitochondrial RNA catabolic process / regulation of mitochondrial translation / rRNA import into mitochondrion / mitochondrial transcription / flagellated sperm motility / mitochondrial translational termination / mitochondrial ribosome assembly / mitochondrial translational elongation ...negative regulation of mitochondrial RNA catabolic process / Mitochondrial RNA degradation / mitochondrial RNA catabolic process / regulation of mitochondrial translation / rRNA import into mitochondrion / mitochondrial transcription / flagellated sperm motility / mitochondrial translational termination / mitochondrial ribosome assembly / mitochondrial translational elongation / translation release factor activity, codon nonspecific / Mitochondrial translation elongation / Mitochondrial translation termination / Mitochondrial translation initiation / translation release factor activity / negative regulation of mitotic nuclear division / mitochondrial large ribosomal subunit / nuclear outer membrane / peptidyl-tRNA hydrolase / mitochondrial ribosome / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / nuclear inner membrane / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / mitochondrial translation / mitochondrion transport along microtubule / beta-tubulin binding / spermatid development / positive regulation of proteolysis / mitochondrial nucleoid / sperm flagellum / ribosomal small subunit binding / single fertilization / anatomical structure morphogenesis / mRNA transport / RNA processing / rescue of stalled ribosome / Mitochondrial protein degradation / cellular response to leukemia inhibitory factor / acrosomal vesicle / condensed nuclear chromosome / mRNA 3'-UTR binding / mitochondrion organization / apoptotic signaling pathway / autophagy / fibrillar center / cell junction / regulation of translation / single-stranded DNA binding / double-stranded RNA binding / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / microtubule binding / small ribosomal subunit rRNA binding / endonuclease activity / nuclear membrane / microtubule / cytoskeleton / tRNA binding / cell population proliferation / mitochondrial inner membrane / negative regulation of translation / rRNA binding / nuclear body / ribosome / structural constituent of ribosome / mitochondrial matrix / protein domain specific binding / translation / ribonucleoprotein complex / nucleotide binding / intracellular membrane-bounded organelle / mRNA binding / apoptotic process / ubiquitin protein ligase binding / GTP binding / positive regulation of DNA-templated transcription / nucleolus / perinuclear region of cytoplasm / mitochondrion / extracellular space / RNA binding / nucleoplasm / nucleus / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.85 Å | ||||||||||||||||||
![]() | Singh, V. / Itoh, Y. / Amunts, A. | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: 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. | ||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 7.4 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | 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 ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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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) ![]() |
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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) ![]() |
#31: RNA chain | Mass: 22354.291 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#32: RNA chain | Mass: 22369.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#33: RNA chain | Mass: 500727.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#34: RNA chain | Mass: 22989.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#91: RNA chain | Mass: 13286.822 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
+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) ![]() |
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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) ![]() |
#67: Protein | Mass: 23352.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#79: Protein | Mass: 12292.333 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#80: Protein | Mass: 23674.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#81: Protein | Mass: 25426.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#88: Protein | Mass: 158098.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#89: Protein | Mass: 78648.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
#90: Protein | Mass: 12371.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() |
+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: ![]() |
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: ![]() |
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 |