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Yorodumi- PDB-7pub: Late assembly intermediate of the Trypanosoma brucei mitoribosoma... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7pub | ||||||||||||
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Title | Late assembly intermediate of the Trypanosoma brucei mitoribosomal small subunit | ||||||||||||
Components |
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Keywords | RIBOSOME / mitoribosome / assembly intermediate / Trypanosoma brucei / small subunit / mt-SSU / SSU | ||||||||||||
Function / homology | Function and homology information photoreactive repair / modulation of formation of structure involved in a symbiotic process / organellar small ribosomal subunit / 3-hydroxyisobutyryl-CoA hydrolase / 3-hydroxyisobutyryl-CoA hydrolase activity / mitochondrial mRNA editing complex / mitochondrial RNA processing / deoxyribodipyrimidine photo-lyase / kinetoplast / deoxyribodipyrimidine photo-lyase activity ...photoreactive repair / modulation of formation of structure involved in a symbiotic process / organellar small ribosomal subunit / 3-hydroxyisobutyryl-CoA hydrolase / 3-hydroxyisobutyryl-CoA hydrolase activity / mitochondrial mRNA editing complex / mitochondrial RNA processing / deoxyribodipyrimidine photo-lyase / kinetoplast / deoxyribodipyrimidine photo-lyase activity / thiosulfate sulfurtransferase activity / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / quorum sensing / translation factor activity, RNA binding / enoyl-CoA hydratase activity / regulation of protein kinase A signaling / ciliary plasm / mRNA stabilization / mitochondrial small ribosomal subunit / fatty acid beta-oxidation / superoxide dismutase / protein kinase A regulatory subunit binding / superoxide dismutase activity / RNA processing / translation initiation factor activity / FAD binding / mitochondrion organization / translational initiation / fatty acid biosynthetic process / transferase activity / ribosome / structural constituent of ribosome / translation / DNA repair / GTPase activity / mRNA binding / GTP binding / mitochondrion / DNA binding / RNA binding / nucleoplasm / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Trypanosoma brucei brucei (eukaryote) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||
Authors | Lenarcic, T. / Leibundgut, M. / Saurer, M. / Ramrath, D.J.F. / Fluegel, T. / Boehringer, D. / Ban, N. | ||||||||||||
Funding support | Switzerland, 3items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2022 Title: Mitoribosomal small subunit maturation involves formation of initiation-like complexes. Authors: Tea Lenarčič / Moritz Niemann / David J F Ramrath / Salvatore Calderaro / Timo Flügel / Martin Saurer / Marc Leibundgut / Daniel Boehringer / Céline Prange / Elke K Horn / André Schneider / Nenad Ban / Abstract: Mitochondrial ribosomes (mitoribosomes) play a central role in synthesizing mitochondrial inner membrane proteins responsible for oxidative phosphorylation. Although mitoribosomes from different ...Mitochondrial ribosomes (mitoribosomes) play a central role in synthesizing mitochondrial inner membrane proteins responsible for oxidative phosphorylation. Although mitoribosomes from different organisms exhibit considerable structural variations, recent insights into mitoribosome assembly suggest that mitoribosome maturation follows common principles and involves a number of conserved assembly factors. To investigate the steps involved in the assembly of the mitoribosomal small subunit (mt-SSU) we determined the cryoelectron microscopy structures of middle and late assembly intermediates of the mitochondrial small subunit (mt-SSU) at 3.6- and 3.7-Å resolution, respectively. We identified five additional assembly factors that together with the mitochondrial initiation factor 2 (mt-IF-2) specifically interact with functionally important regions of the rRNA, including the decoding center, thereby preventing premature mRNA or large subunit binding. Structural comparison of assembly intermediates with mature mt-SSU combined with RNAi experiments suggests a noncanonical role of mt-IF-2 and a stepwise assembly process, where modular exchange of ribosomal proteins and assembly factors together with mt-IF-2 ensure proper 9S rRNA folding and protein maturation during the final steps of assembly. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7pub.cif.gz | 4.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7pub.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 7pub.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7pub_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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Full document | 7pub_full_validation.pdf.gz | 1.8 MB | Display | |
Data in XML | 7pub_validation.xml.gz | 524.1 KB | Display | |
Data in CIF | 7pub_validation.cif.gz | 865.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pu/7pub ftp://data.pdbj.org/pub/pdb/validation_reports/pu/7pub | HTTPS FTP |
-Related structure data
Related structure data | 13661MC 7puaC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-RNA chain , 1 types, 1 molecules CA
#1: RNA chain | Mass: 198441.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 / References: GenBank: 13740 |
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+Protein , 67 types, 67 molecules CCCECFCHCICJCKCLCNCOCPCQCRCSCUCaCbCdCgCiCjCkCmCnCpCqCrCvDADB...
-Protein/peptide , 7 types, 8 molecules U6UJU7UFUGUIUKUL
#68: Protein/peptide | Mass: 1805.216 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 #69: Protein/peptide | | Mass: 3422.209 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 #71: Protein/peptide | | Mass: 3337.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 #72: Protein/peptide | | Mass: 1124.378 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 #73: Protein/peptide | | Mass: 869.063 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 #74: Protein/peptide | | Mass: 273.330 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 #75: Protein/peptide | | Mass: 1720.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Trypanosoma brucei brucei (eukaryote) / Strain: Tb427.10 |
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-Non-polymers , 8 types, 20 molecules
#76: Chemical | ChemComp-MG / #77: Chemical | ChemComp-ATP / | #78: Chemical | ChemComp-ZN / #79: Chemical | ChemComp-UTP / | #80: Chemical | ChemComp-FAD / | #81: Chemical | ChemComp-GDP / | #82: Chemical | ChemComp-PO4 / | #83: Water | ChemComp-HOH / | |
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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 |
-Sample preparation
Component | Name: Late assembly intermediate of the Trypanosoma brucei mitoribosomal small subunit Type: RIBOSOME / Entity ID: #1-#75 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Trypanosoma brucei brucei (eukaryote) |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/2 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 98 % / Chamber temperature: 277 K |
-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: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||
3D reconstruction | Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17391 / Symmetry type: POINT |