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- EMDB-12867: Structure of a human mitochondrial ribosome large subunit assembl... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-12867 | ||||||||||||||||||
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Title | Structure of a human mitochondrial ribosome large subunit assembly intermediate in complex with GTPBP6. | ||||||||||||||||||
![]() | Global refinement map. | ||||||||||||||||||
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Function / homology | ![]() negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / Complex I biogenesis / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / rRNA import into mitochondrion / Respiratory electron transport / mitochondrial translational termination / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding ...negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / Complex I biogenesis / negative regulation of ribosome biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / rRNA import into mitochondrion / Respiratory electron transport / mitochondrial translational termination / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / protein lipoylation / translation release factor activity, codon nonspecific / Mitochondrial translation elongation / Mitochondrial translation termination / positive regulation of mitochondrial translation / Mitochondrial translation initiation / mitochondrial translational elongation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||
Method | ![]() ![]() | ||||||||||||||||||
![]() | Hillen HS / Lavdovskaia E / Nadler F / Hanitsch E / Linden A / Bohnsack KE / Urlaub H / Richter-Dennerlein R | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling. Authors: Hauke S Hillen / Elena Lavdovskaia / Franziska Nadler / Elisa Hanitsch / Andreas Linden / Katherine E Bohnsack / Henning Urlaub / Ricarda Richter-Dennerlein / ![]() Abstract: Ribosome biogenesis requires auxiliary factors to promote folding and assembly of ribosomal proteins and RNA. Particularly, maturation of the peptidyl transferase center (PTC) is mediated by ...Ribosome biogenesis requires auxiliary factors to promote folding and assembly of ribosomal proteins and RNA. Particularly, maturation of the peptidyl transferase center (PTC) is mediated by conserved GTPases, but the molecular basis is poorly understood. Here, we define the mechanism of GTPase-driven maturation of the human mitochondrial large ribosomal subunit (mtLSU) using endogenous complex purification, in vitro reconstitution and cryo-EM. Structures of transient native mtLSU assembly intermediates that accumulate in GTPBP6-deficient cells reveal how the biogenesis factors GTPBP5, MTERF4 and NSUN4 facilitate PTC folding. Addition of recombinant GTPBP6 reconstitutes late mtLSU biogenesis in vitro and shows that GTPBP6 triggers a molecular switch and progression to a near-mature PTC state. Additionally, cryo-EM analysis of GTPBP6-treated mature mitochondrial ribosomes reveals the structural basis for the dual-role of GTPBP6 in ribosome biogenesis and recycling. Together, these results provide a framework for understanding step-wise PTC folding as a critical conserved quality control checkpoint. #1: ![]() Title: Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling Authors: Hillen HS / Lavdovskaia E / Nadler F / Hanitsch E / Linden A / Bohnsack KE / Urlaub H / Richter-Dennerlein R | ||||||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 112.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 76.7 KB 76.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.4 KB | Display | ![]() |
Images | ![]() | 96.2 KB | ||
Masks | ![]() | 163.6 MB | ![]() | |
Others | ![]() ![]() ![]() | 14.4 MB 113.3 MB 113.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 442.6 KB | Display | ![]() |
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Full document | ![]() | 441.7 KB | Display | |
Data in XML | ![]() | 20.2 KB | Display | |
Data in CIF | ![]() | 26.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7of2MC ![]() 7of0C ![]() 7of3C ![]() 7of4C ![]() 7of5C ![]() 7of6C ![]() 7of7C M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Global refinement map. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Density Histograms |
-Additional map: Post-processed map.
File | emd_12867_additional_1.map | ||||||||||||
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Annotation | Post-processed map. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Refinement half-map 1.
File | emd_12867_half_map_1.map | ||||||||||||
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Annotation | Refinement half-map 1. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Refinement half-map 2.
File | emd_12867_half_map_2.map | ||||||||||||
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Annotation | Refinement half-map 2. | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Human mitochondrial ribosome large subunit assembly intermediate ...
+Supramolecule #1: Human mitochondrial ribosome large subunit assembly intermediate ...
+Macromolecule #1: 39S ribosomal protein L32, mitochondrial
+Macromolecule #2: 39S ribosomal protein L33, mitochondrial
+Macromolecule #3: 39S ribosomal protein L34, mitochondrial
+Macromolecule #4: 39S ribosomal protein L35, mitochondrial
+Macromolecule #5: 39S ribosomal protein L36, mitochondrial
+Macromolecule #6: 39S ribosomal protein L37, mitochondrial
+Macromolecule #7: 39S ribosomal protein L38, mitochondrial
+Macromolecule #8: 39S ribosomal protein L39, mitochondrial
+Macromolecule #9: 39S ribosomal protein L40, mitochondrial
+Macromolecule #10: 39S ribosomal protein L41, mitochondrial
+Macromolecule #13: Putative GTP-binding protein 6
+Macromolecule #14: 39S ribosomal protein L2, mitochondrial
+Macromolecule #15: 39S ribosomal protein L3, mitochondrial
+Macromolecule #16: 39S ribosomal protein L4, mitochondrial
+Macromolecule #17: 39S ribosomal protein L9, mitochondrial
+Macromolecule #18: 39S ribosomal protein L10, mitochondrial
+Macromolecule #19: 39S ribosomal protein L11, mitochondrial
+Macromolecule #20: 39S ribosomal protein L13, mitochondrial
+Macromolecule #21: 39S ribosomal protein L14, mitochondrial
+Macromolecule #22: 39S ribosomal protein L15, mitochondrial
+Macromolecule #23: 39S ribosomal protein L16, mitochondrial
+Macromolecule #24: 39S ribosomal protein L17, mitochondrial
+Macromolecule #25: 39S ribosomal protein L18, mitochondrial
+Macromolecule #26: 39S ribosomal protein L19, mitochondrial
+Macromolecule #27: 39S ribosomal protein L20, mitochondrial
+Macromolecule #28: 39S ribosomal protein L21, mitochondrial
+Macromolecule #29: 39S ribosomal protein L22, mitochondrial
+Macromolecule #30: 39S ribosomal protein L23, mitochondrial
+Macromolecule #31: 39S ribosomal protein L24, mitochondrial
+Macromolecule #32: 39S ribosomal protein L27, mitochondrial
+Macromolecule #33: 39S ribosomal protein L28, mitochondrial
+Macromolecule #34: 39S ribosomal protein L47, mitochondrial
+Macromolecule #35: 39S ribosomal protein L30, mitochondrial
+Macromolecule #36: 39S ribosomal protein L42, mitochondrial
+Macromolecule #37: 39S ribosomal protein L43, mitochondrial
+Macromolecule #38: 39S ribosomal protein L44, mitochondrial
+Macromolecule #39: 39S ribosomal protein L45, mitochondrial
+Macromolecule #40: 39S ribosomal protein L46, mitochondrial
+Macromolecule #41: 39S ribosomal protein L48, mitochondrial
+Macromolecule #42: 39S ribosomal protein L49, mitochondrial
+Macromolecule #43: 39S ribosomal protein L50, mitochondrial
+Macromolecule #44: 39S ribosomal protein L51, mitochondrial
+Macromolecule #45: 39S ribosomal protein L52, mitochondrial
+Macromolecule #46: 39S ribosomal protein L53, mitochondrial
+Macromolecule #47: 39S ribosomal protein L54, mitochondrial
+Macromolecule #48: 39S ribosomal protein L55, mitochondrial
+Macromolecule #49: Ribosomal protein 63, mitochondrial
+Macromolecule #50: Peptidyl-tRNA hydrolase ICT1, mitochondrial
+Macromolecule #51: Growth arrest and DNA damage-inducible proteins-interacting protein 1
+Macromolecule #52: 39S ribosomal protein S18a, mitochondrial
+Macromolecule #53: 39S ribosomal protein S30, mitochondrial
+Macromolecule #54: Mitochondrial assembly of ribosomal large subunit protein 1
+Macromolecule #55: MIEF1 upstream open reading frame protein
+Macromolecule #56: Acyl carrier protein, mitochondrial
+Macromolecule #11: 16S ribosomal RNA
+Macromolecule #12: mitochondrial tRNAVal
+Macromolecule #57: ZINC ION
+Macromolecule #58: MAGNESIUM ION
+Macromolecule #59: GUANOSINE-5'-TRIPHOSPHATE
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R3.5/1 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 0.25 nm |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated defocus max: 2.1 µm / Calibrated defocus min: 0.3 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD![]() |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 37.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |