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Yorodumi- PDB-6hix: Cryo-EM structure of the Trypanosoma brucei mitochondrial ribosom... -
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-Basic information
Entry | Database: PDB / ID: 6hix | |||||||||
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Title | Cryo-EM structure of the Trypanosoma brucei mitochondrial ribosome - This entry contains the large mitoribosomal subunit | |||||||||
Components |
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Keywords | RIBOSOME / mitoribosome / translation / Trypanosoma / large ribosomal subunit / 12S rRNA / ribosomal protein | |||||||||
Function / homology | Function and homology information organellar large ribosomal subunit / mitochondrial mRNA editing complex / mitochondrial RNA processing / kinetoplast / nuclear lumen / mitochondrial large ribosomal subunit / ciliary plasm / mitochondrial ribosome / mitochondrial translation / post-transcriptional regulation of gene expression ...organellar large ribosomal subunit / mitochondrial mRNA editing complex / mitochondrial RNA processing / kinetoplast / nuclear lumen / mitochondrial large ribosomal subunit / ciliary plasm / mitochondrial ribosome / mitochondrial translation / post-transcriptional regulation of gene expression / cyclosporin A binding / ciliary basal body / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / large ribosomal subunit / protein folding / large ribosomal subunit rRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / mitochondrion / RNA binding / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Trypanosoma brucei brucei (eukaryote) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.39 Å | |||||||||
Authors | Ramrath, D.J.F. / Niemann, M. / Leibundgut, M. / Bieri, P. / Prange, C. / Horn, K. / Leitner, A. / Boehringer, D. / Schneider, A. / Ban, N. | |||||||||
Funding support | Switzerland, 1items
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Citation | Journal: Science / Year: 2018 Title: Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes. Authors: David J F Ramrath / Moritz Niemann / Marc Leibundgut / Philipp Bieri / Céline Prange / Elke K Horn / Alexander Leitner / Daniel Boehringer / André Schneider / Nenad Ban / Abstract: Ribosomal RNA (rRNA) plays key functional and architectural roles in ribosomes. Using electron microscopy, we determined the atomic structure of a highly divergent ribosome found in mitochondria of , ...Ribosomal RNA (rRNA) plays key functional and architectural roles in ribosomes. Using electron microscopy, we determined the atomic structure of a highly divergent ribosome found in mitochondria of , a unicellular parasite that causes sleeping sickness in humans. The trypanosomal mitoribosome features the smallest rRNAs and contains more proteins than all known ribosomes. The structure shows how the proteins have taken over the role of architectural scaffold from the rRNA: They form an autonomous outer shell that surrounds the entire particle and stabilizes and positions the functionally important regions of the rRNA. Our results also reveal the "minimal" set of conserved rRNA and protein components shared by all ribosomes that help us define the most essential functional elements. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
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PDBx/mmCIF format | 6hix.cif.gz | 3.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6hix.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6hix.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6hix_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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Full document | 6hix_full_validation.pdf.gz | 2 MB | Display | |
Data in XML | 6hix_validation.xml.gz | 345 KB | Display | |
Data in CIF | 6hix_validation.cif.gz | 574.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hi/6hix ftp://data.pdbj.org/pub/pdb/validation_reports/hi/6hix | HTTPS FTP |
-Related structure data
Related structure data | 0231MC 0229C 0230C 0232C 0233C 6hivC 6hiwC 6hiyC 6hizC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
+Protein , 63 types, 63 molecules A0A1A2A3A4A5A6A8A9AIAJAPATAUAVAWAXAYAbAdAeAfAgAjAlAoApAtAvAB...
-Ribosomal protein ... , 3 types, 3 molecules AEAFAK
#10: Protein | Mass: 55073.699 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb927.3.5610 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q580R4 |
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#11: Protein | Mass: 53156.664 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: TEOVI_000582800 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: A0A1G4HYD1 |
#14: Protein | Mass: 40252.750 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb927.2.4740, Tb927.2.4890 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q586R9 |
-50S ribosomal protein ... , 3 types, 3 molecules ANAQAR
#15: Protein | Mass: 24341.309 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb927.4.1070 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q580D5 |
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#17: Protein | Mass: 19158.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb927.7.3960 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q57UM6 |
#18: Protein | Mass: 35117.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb927.8.5860 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q57YI7 |
-Protein/peptide , 14 types, 19 molecules ACADAGUAUBUCUHUEUFUGUNUIUKULUMUUUVUXUW
#37: Protein/peptide | Mass: 2008.194 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #38: Protein/peptide | | Mass: 1937.116 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #74: Protein/peptide | | Mass: 3932.839 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #75: Protein/peptide | | Mass: 3422.209 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #76: Protein/peptide | Mass: 1039.273 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #78: Protein/peptide | | Mass: 1890.321 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #79: Protein/peptide | Mass: 2060.531 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #80: Protein/peptide | | Mass: 1464.797 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #81: Protein/peptide | | Mass: 869.063 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #82: Protein/peptide | | Mass: 1294.587 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #83: Protein/peptide | | Mass: 528.644 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #84: Protein/peptide | | Mass: 954.168 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #85: Protein/peptide | Mass: 698.854 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 #86: Protein/peptide | | Mass: 613.749 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: unassigned residues built as UNK / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 |
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-RNA chain , 1 types, 1 molecules AA
#39: RNA chain | Mass: 376748.500 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: GenBank: 343546 |
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-Peptidyl-prolyl cis-trans ... , 2 types, 2 molecules BQBZ
#56: Protein | Mass: 25579.004 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb927.7.3430 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q57WF8, peptidylprolyl isomerase |
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#65: Protein | Mass: 20542.291 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: residues 46-64 built as polyalanines / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 / Gene: Tb11.01.1215 / Production host: Trypanosoma brucei brucei (eukaryote) / Strain (production host): Lister 427 / References: UniProt: Q383Y4, peptidylprolyl isomerase |
-Non-polymers , 3 types, 14 molecules
#87: Chemical | ChemComp-ZN / #88: Chemical | ChemComp-NAD / | #89: Chemical | ChemComp-MG / |
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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
Component | Name: large subunit of the T. brucei mitoribosome / Type: RIBOSOME / Entity ID: #1-#86 / Source: NATURAL |
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Molecular weight | Value: 1.9 MDa / Experimental value: YES |
Source (natural) | Organism: Trypanosoma brucei brucei (eukaryote) / Strain: Lister 427 |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 98 % / Chamber temperature: 278 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 |
Image recording | Electron dose: 40 e/Å2 / Detector mode: INTEGRATING / 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: 3.39 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 31619 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | B value: 52.2 / Protocol: AB INITIO MODEL Details: We used Coot and O ofr initial model building and refined the structure using PHENIX |