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- EMDB-12763: Human mitochondrial ribosome large subunit assembly intermediate ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-12763 | |||||||||
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Title | Human mitochondrial ribosome large subunit assembly intermediate with MTERF4-NSUN4, MRM2, MTG1, the MALSU module, GTPBP5 and mtEF-Tu | |||||||||
![]() | Locally filtered map from cryoSPARC non-uniform refinement | |||||||||
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Function / homology | ![]() mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / rRNA modification in the mitochondrion / tRNA (cytidine-5-)-methyltransferase activity / mitochondrial RNA modification / mitochondrial RNA catabolic process / regulation of mitochondrial translation / rRNA 2'-O-methylation / negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly ...mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / rRNA modification in the mitochondrion / tRNA (cytidine-5-)-methyltransferase activity / mitochondrial RNA modification / mitochondrial RNA catabolic process / regulation of mitochondrial translation / rRNA 2'-O-methylation / negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / rRNA (uridine-2'-O-)-methyltransferase activity / SARS-CoV-2 modulates autophagy / rRNA (cytosine-C5-)-methyltransferase activity / negative regulation of ribosome biogenesis / Complex I biogenesis / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / RNA methylation / Respiratory electron transport / RNA methyltransferase activity / rRNA methyltransferase activity / mitochondrial transcription / mitochondrial translational elongation / mitochondrial translational termination / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / positive regulation of mitochondrial translation / protein targeting to mitochondrion / camera-type eye development / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit / mitochondrial fission / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / mitochondrial ribosome / peptidyl-tRNA hydrolase / rRNA methylation / mitochondrial small ribosomal subunit / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / mitochondrial translation / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / iron-sulfur cluster assembly / acyl binding / acyl carrier activity / ribosomal large subunit binding / mitochondrial nucleoid / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / proton motive force-driven mitochondrial ATP synthesis / translational elongation / respiratory chain complex I / anatomical structure morphogenesis / translation elongation factor activity / RNA processing / rescue of stalled ribosome / Mitochondrial protein degradation / cellular response to leukemia inhibitory factor / aerobic respiration / Transferases; Transferring one-carbon groups; Methyltransferases / ribosomal large subunit biogenesis / fatty acid binding / methyltransferase activity / mitochondrial membrane / fibrillar center / rRNA processing / fatty acid biosynthetic process / double-stranded RNA binding / cell junction / ribosome biogenesis / large ribosomal subunit / heart development / small ribosomal subunit rRNA binding / double-stranded DNA binding / large ribosomal subunit rRNA binding / endonuclease activity / response to ethanol / mitochondrial outer membrane / mitochondrial inner membrane / nuclear body / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / mitochondrial matrix / translation / protein domain specific binding / ribonucleoprotein complex / GTPase activity / nucleotide binding / mRNA binding / synapse / calcium ion binding / apoptotic process / regulation of DNA-templated transcription / nucleolus Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
![]() | Valentin Gese G / Hallberg BM | |||||||||
![]() | ![]() Title: Structural basis for late maturation steps of the human mitoribosomal large subunit. Authors: Miriam Cipullo / Genís Valentín Gesé / Anas Khawaja / B Martin Hällberg / Joanna Rorbach / ![]() ![]() Abstract: Mitochondrial ribosomes (mitoribosomes) synthesize a critical set of proteins essential for oxidative phosphorylation. Therefore, mitoribosomal function is vital to the cellular energy supply. ...Mitochondrial ribosomes (mitoribosomes) synthesize a critical set of proteins essential for oxidative phosphorylation. Therefore, mitoribosomal function is vital to the cellular energy supply. Mitoribosome biogenesis follows distinct molecular pathways that remain poorly understood. Here, we determine the cryo-EM structures of mitoribosomes isolated from human cell lines with either depleted or overexpressed mitoribosome assembly factor GTPBP5, allowing us to capture consecutive steps during mitoribosomal large subunit (mt-LSU) biogenesis. Our structures provide essential insights into the last steps of 16S rRNA folding, methylation and peptidyl transferase centre (PTC) completion, which require the coordinated action of nine assembly factors. We show that mammalian-specific MTERF4 contributes to the folding of 16S rRNA, allowing 16 S rRNA methylation by MRM2, while GTPBP5 and NSUN4 promote fine-tuning rRNA rearrangements leading to PTC formation. Moreover, our data reveal an unexpected involvement of the elongation factor mtEF-Tu in mt-LSU assembly, where mtEF-Tu interacts with GTPBP5, similar to its interaction with tRNA during translational elongation. | |||||||||
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 | ![]() | 52 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 81.1 KB 81.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 20.8 KB | Display | ![]() |
Images | ![]() | 61.4 KB | ||
Others | ![]() ![]() ![]() | 47.9 MB 52.1 MB 52.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 569.2 KB | Display | ![]() |
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Full document | ![]() | 568.4 KB | Display | |
Data in XML | ![]() | 18.5 KB | Display | |
Data in CIF | ![]() | 27.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7o9kMC ![]() 7o9mC 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 | Locally filtered map from cryoSPARC non-uniform refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.02 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: Map post-processed with DeepEMhancer
File | emd_12763_additional_1.map | ||||||||||||
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Annotation | Map post-processed with DeepEMhancer | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map A
File | emd_12763_half_map_1.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B
File | emd_12763_half_map_2.map | ||||||||||||
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Annotation | Half map B | ||||||||||||
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Density Histograms |
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Sample components
+Entire : 55S subunit assembly intermediate
+Supramolecule #1: 55S subunit assembly intermediate
+Macromolecule #1: 39S ribosomal protein L32, mitochondrial
+Macromolecule #2: 39S ribosomal protein L42, mitochondrial
+Macromolecule #3: 39S ribosomal protein L33, mitochondrial
+Macromolecule #4: 39S ribosomal protein L34, mitochondrial
+Macromolecule #5: 39S ribosomal protein L35, mitochondrial
+Macromolecule #6: 39S ribosomal protein L36, mitochondrial
+Macromolecule #7: 39S ribosomal protein L37, mitochondrial
+Macromolecule #8: 39S ribosomal protein L38, mitochondrial
+Macromolecule #9: 39S ribosomal protein L39, mitochondrial
+Macromolecule #10: 39S ribosomal protein L40, mitochondrial
+Macromolecule #11: 39S ribosomal protein L41, mitochondrial
+Macromolecule #13: 5-methylcytosine rRNA methyltransferase NSUN4
+Macromolecule #15: Transcription termination factor 4, mitochondrial
+Macromolecule #16: Mitochondrial ribosome-associated GTPase 1
+Macromolecule #17: 39S ribosomal protein L2, mitochondrial
+Macromolecule #18: 39S ribosomal protein L3, mitochondrial
+Macromolecule #19: 39S ribosomal protein L4, mitochondrial
+Macromolecule #20: 39S ribosomal protein L12, mitochondrial
+Macromolecule #21: Mitochondrial ribosome-associated GTPase 2
+Macromolecule #22: 39S ribosomal protein L9, mitochondrial
+Macromolecule #23: 39S ribosomal protein L10, mitochondrial
+Macromolecule #24: 39S ribosomal protein L11, mitochondrial
+Macromolecule #25: 39S ribosomal protein L13, mitochondrial
+Macromolecule #26: 39S ribosomal protein L14, mitochondrial
+Macromolecule #27: 39S ribosomal protein L15, mitochondrial
+Macromolecule #28: 39S ribosomal protein L16, mitochondrial
+Macromolecule #29: 39S ribosomal protein L17, mitochondrial
+Macromolecule #30: Mitochondrial ribosomal protein L18, isoform CRA_b
+Macromolecule #31: 39S ribosomal protein L19, mitochondrial
+Macromolecule #32: 39S ribosomal protein L20, mitochondrial
+Macromolecule #33: 39S ribosomal protein L21, mitochondrial
+Macromolecule #34: 39S ribosomal protein L22, mitochondrial
+Macromolecule #35: 39S ribosomal protein L23, mitochondrial
+Macromolecule #36: 39S ribosomal protein L24, mitochondrial
+Macromolecule #37: 39S ribosomal protein L27, mitochondrial
+Macromolecule #38: 39S ribosomal protein L28, mitochondrial
+Macromolecule #39: 39S ribosomal protein L47, mitochondrial
+Macromolecule #40: 39S ribosomal protein L30, mitochondrial
+Macromolecule #41: 39S ribosomal protein L43, mitochondrial
+Macromolecule #42: 39S ribosomal protein L44, mitochondrial
+Macromolecule #43: 39S ribosomal protein L45, mitochondrial
+Macromolecule #44: 39S ribosomal protein L46, mitochondrial
+Macromolecule #45: 39S ribosomal protein L48, mitochondrial
+Macromolecule #46: 39S ribosomal protein L49, mitochondrial
+Macromolecule #47: 39S ribosomal protein L50, mitochondrial
+Macromolecule #48: 39S ribosomal protein L51, mitochondrial
+Macromolecule #49: 39S ribosomal protein L52, mitochondrial
+Macromolecule #50: 39S ribosomal protein L53, mitochondrial
+Macromolecule #51: 39S ribosomal protein L54, mitochondrial
+Macromolecule #52: 39S ribosomal protein L55, mitochondrial
+Macromolecule #53: rRNA methyltransferase 2, mitochondrial
+Macromolecule #54: Ribosomal protein 63, mitochondrial
+Macromolecule #55: Peptidyl-tRNA hydrolase ICT1, mitochondrial
+Macromolecule #56: Growth arrest and DNA damage-inducible proteins-interacting protein 1
+Macromolecule #57: 39S ribosomal protein S18a, mitochondrial
+Macromolecule #58: 39S ribosomal protein S30, mitochondrial
+Macromolecule #59: Elongation factor Tu, mitochondrial
+Macromolecule #60: Mitochondrial assembly of ribosomal large subunit protein 1
+Macromolecule #61: MIEF1 upstream open reading frame protein
+Macromolecule #62: Acyl carrier protein, mitochondrial
+Macromolecule #63: UNK
+Macromolecule #12: 16S rRNA
+Macromolecule #14: MT-TRNAVAL
+Macromolecule #64: ZINC ION
+Macromolecule #65: MAGNESIUM ION
+Macromolecule #66: S-ADENOSYLMETHIONINE
+Macromolecule #67: GUANOSINE-5'-DIPHOSPHATE
+Macromolecule #68: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #69: S-ADENOSYL-L-HOMOCYSTEINE
+Macromolecule #70: 4'-PHOSPHOPANTETHEINE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 10 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 49.2 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 20.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |