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Open data
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Basic information
Entry | Database: PDB / ID: 9hny | |||||||||
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Title | Mitoribosomal small subunit in complex with Mettl15 and Mettl17 | |||||||||
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![]() | RIBOSOME / Mitochondrial ribosome / METTL15 / METTL17 / RbfA / Trypanosoma brucei | |||||||||
Function / homology | ![]() rRNA (cytosine-N4-)-methyltransferase activity / mitochondrial mRNA editing complex / mitochondrial RNA processing / tRNA pseudouridine synthesis / pseudouridine synthase activity / ATP-activated inward rectifier potassium channel activity / kinetoplast / thiosulfate-cyanide sulfurtransferase activity / rRNA base methylation / response to arsenic-containing substance ...rRNA (cytosine-N4-)-methyltransferase activity / mitochondrial mRNA editing complex / mitochondrial RNA processing / tRNA pseudouridine synthesis / pseudouridine synthase activity / ATP-activated inward rectifier potassium channel activity / kinetoplast / thiosulfate-cyanide sulfurtransferase activity / rRNA base methylation / response to arsenic-containing substance / ciliary plasm / ribonuclease P activity / tRNA 5'-leader removal / nuclear lumen / mRNA stabilization / mitochondrial small ribosomal subunit / acyl binding / acyl carrier activity / iron-sulfur cluster binding / catalytic activity / voltage-gated potassium channel activity / RNA processing / voltage-gated potassium channel complex / methyltransferase activity / mitochondrion organization / potassium ion transport / protein homooligomerization / NAD binding / fatty acid biosynthetic process / NADP binding / ribosome / structural constituent of ribosome / mitochondrial matrix / translation / ribonucleoprotein complex / mRNA binding / mitochondrion / RNA binding / nucleoplasm / metal ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Zgadzay, Y. / Aibara, S. / Gahura, O. / Amunts, A. | |||||||||
Funding support | European Union, ![]()
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![]() | ![]() Title: Mettl15-Mettl17 modulates the transition from early to late pre-mitoribosome. Authors: Yury Zgadzay / Claudio Mirabello / George Wanes / Tomáš Pánek / Prashant Chauhan / Björn Nystedt / Alena Zíková / Paul C Whitford / Ondřej Gahura / Alexey Amunts / ![]() ![]() ![]() ![]() Abstract: The assembly of the mitoribosomal small subunit involves folding and modification of rRNA, and its association with mitoribosomal proteins. This process is assisted by a dynamic network of assembly ...The assembly of the mitoribosomal small subunit involves folding and modification of rRNA, and its association with mitoribosomal proteins. This process is assisted by a dynamic network of assembly factors. Conserved methyltransferases Mettl15 and Mettl17 act on the solvent-exposed surface of rRNA. Binding of Mettl17 is associated with the early assembly stage, whereas Mettl15 is involved in the late stage, but the mechanism of transition between the two was unclear. Here, we integrate structural data from with mammalian homologs and molecular dynamics simulations. We reveal how the interplay of Mettl15 and Mettl17 in intermediate steps links the distinct stages of small subunit assembly. The analysis suggests a model wherein Mettl17 acts as a platform for Mettl15 recruitment. Subsequent release of Mettl17 allows a conformational change of Mettl15 for substrate recognition. Upon methylation, Mettl15 adopts a loosely bound state which ultimately leads to its replacement by initiation factors, concluding the assembly. Together, our results indicate that assembly factors Mettl15 and Mettl17 cooperate to regulate the biogenesis process, and present a structural data resource for understanding molecular adaptations of assembly factors in mitoribosome. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 9.2 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | M: map data used to model this data |
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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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Components
-RNA chain , 1 types, 1 molecules CA
#1: RNA chain | Mass: 198135.234 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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+Protein , 74 types, 80 molecules CCCECFCHCICJCKCNCPCQCSCaCbCdCiCjCkCnCpDBDCDDDFDGDHDIDJDKDLDO...
-Mitochondrial ... , 6 types, 6 molecules COCRCgDEF1FK
#10: Protein | Mass: 50401.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#13: Protein | Mass: 36988.691 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#18: Protein | Mass: 56334.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#27: Protein | Mass: 84998.234 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#45: Protein | Mass: 119799.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#63: Protein | Mass: 41236.418 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-PPR long domain-containing ... , 2 types, 2 molecules FDFX
#56: Protein | Mass: 65049.215 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#71: Protein | Mass: 26936.748 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein/peptide , 14 types, 16 molecules UAUBUCUFUGUJUIUKULUMUQUNUOUPUkUl
#80: Protein/peptide | Mass: 2315.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||
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#81: Protein/peptide | Mass: 528.644 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||
#82: Protein/peptide | Mass: 869.063 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||
#83: Protein/peptide | Mass: 954.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||
#84: Protein/peptide | Mass: 1379.692 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #85: Protein/peptide | | Mass: 698.854 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #86: Protein/peptide | | Mass: 2060.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #87: Protein/peptide | | Mass: 1890.321 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #88: Protein/peptide | Mass: 783.958 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #89: Protein/peptide | | Mass: 613.749 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #90: Protein/peptide | | Mass: 2571.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #91: Protein/peptide | | Mass: 3847.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #96: Protein/peptide | | Mass: 2656.265 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #97: Protein/peptide | | Mass: 1209.482 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 7 types, 11 molecules 












#98: Chemical | ChemComp-GTP / | ||||||
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#99: Chemical | ChemComp-MG / | ||||||
#100: Chemical | ChemComp-SF4 / | ||||||
#101: Chemical | #102: Chemical | ChemComp-ACO / | #103: Chemical | ChemComp-ZN / #104: Chemical | ChemComp-PO4 / | |
-Details
Has ligand of interest | Y |
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Has protein modification | N |
-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: Mitoribosomal small subunit in complex with Mettl15 and Mettl17 Type: RIBOSOME / Entity ID: #1-#97 / 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-PROPANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: DARK FIELD / Nominal defocus max: 3200 nm / Nominal defocus min: 2000 nm |
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: PHENIX / Version: 1.19rc4_4035: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 104838 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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