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Yorodumi- EMDB-11645: Structure of the split human mitoribosomal large subunit with P-a... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-11645 | ||||||||||||
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| Title | Structure of the split human mitoribosomal large subunit with P-and E-site mt-tRNAs | ||||||||||||
Map data | postprocessed masked map | ||||||||||||
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| Function / homology | Function and homology informationnegative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / protein lipoylation / negative regulation of ribosome biogenesis / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / positive regulation of mitochondrial translation / Respiratory electron transport / mitochondrial translational termination ...negative regulation of mitochondrial translation / mitochondrial large ribosomal subunit assembly / protein lipoylation / negative regulation of ribosome biogenesis / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / positive regulation of mitochondrial translation / Respiratory electron transport / mitochondrial translational termination / mitochondrial translational elongation / Mitochondrial translation elongation / Mitochondrial translation termination / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / translation release factor activity / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit / mitochondrial fission / peptidyl-tRNA hydrolase / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / mitochondrial ribosome / mitochondrial small ribosomal subunit / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / peptidyl-tRNA hydrolase activity / mitochondrial translation / [2Fe-2S] cluster assembly / iron-sulfur cluster assembly / acyl binding / ribosomal large subunit binding / acyl carrier activity / mitochondrial respiratory chain complex I assembly / proton motive force-driven mitochondrial ATP synthesis / mitochondrial electron transport, NADH to ubiquinone / anatomical structure morphogenesis / respiratory chain complex I / RNA processing / rescue of stalled cytosolic ribosome / Mitochondrial protein degradation / aerobic respiration / fatty acid binding / cellular response to leukemia inhibitory factor / ribosomal large subunit biogenesis / mitochondrial membrane / fibrillar center / fatty acid biosynthetic process / cell junction / regulation of translation / double-stranded RNA binding / large ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / tRNA binding / negative regulation of translation / mitochondrial inner membrane / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / mRNA binding / apoptotic process / calcium ion binding / nucleolus / structural molecule activity / mitochondrion / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) / ![]() Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) / human (human) / ![]() Thermus thermophilus HB27 (bacteria) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
Authors | Desai N / Yang H / Chandrasekaran V / Kazi R / Minczuk M / Ramakrishnan V | ||||||||||||
| Funding support | United Kingdom, 3 items
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Citation | Journal: Science / Year: 2020Title: Elongational stalling activates mitoribosome-associated quality control. Authors: Nirupa Desai / Hanting Yang / Viswanathan Chandrasekaran / Razina Kazi / Michal Minczuk / V Ramakrishnan / ![]() Abstract: The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a ...The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase. | ||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_11645.map.gz | 41.9 MB | EMDB map data format | |
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| Header (meta data) | emd-11645-v30.xml emd-11645.xml | 84.5 KB 84.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_11645_fsc.xml | 18 KB | Display | FSC data file |
| Images | emd_11645.png | 190.5 KB | ||
| Masks | emd_11645_msk_1.map | 512 MB | Mask map | |
| Others | emd_11645_additional_1.map.gz emd_11645_half_map_1.map.gz emd_11645_half_map_2.map.gz | 412.6 MB 413.9 MB 414 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11645 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11645 | HTTPS FTP |
-Validation report
| Summary document | emd_11645_validation.pdf.gz | 714.3 KB | Display | EMDB validaton report |
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| Full document | emd_11645_full_validation.pdf.gz | 713.9 KB | Display | |
| Data in XML | emd_11645_validation.xml.gz | 26.2 KB | Display | |
| Data in CIF | emd_11645_validation.cif.gz | 35.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11645 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11645 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7a5jMC ![]() 7a5fC ![]() 7a5gC ![]() 7a5hC ![]() 7a5iC ![]() 7a5kC 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 | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_11645.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | postprocessed masked map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.25938 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
| File | emd_11645_msk_1.map | ||||||||||||
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-Additional map: refined map
| File | emd_11645_additional_1.map | ||||||||||||
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| Annotation | refined map | ||||||||||||
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-Half map: Half2 map
| File | emd_11645_half_map_1.map | ||||||||||||
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| Annotation | Half2 map | ||||||||||||
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-Half map: Half1 map
| File | emd_11645_half_map_2.map | ||||||||||||
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| Annotation | Half1 map | ||||||||||||
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Sample components
+Entire : human mitoribosome
+Supramolecule #1: human mitoribosome
+Supramolecule #2: ribosome
+Supramolecule #3: 50S ribosomal protein L1
+Macromolecule #1: 39S ribosomal protein L2, mitochondrial
+Macromolecule #2: 39S ribosomal protein L3, mitochondrial
+Macromolecule #3: 39S ribosomal protein L4, mitochondrial
+Macromolecule #4: 39S ribosomal protein L9, mitochondrial
+Macromolecule #5: 39S ribosomal protein L10, mitochondrial
+Macromolecule #6: 39S ribosomal protein L11, mitochondrial
+Macromolecule #7: 39S ribosomal protein L13, mitochondrial
+Macromolecule #8: 39S ribosomal protein L14, mitochondrial
+Macromolecule #9: 39S ribosomal protein L15, mitochondrial
+Macromolecule #10: 39S ribosomal protein L16, mitochondrial
+Macromolecule #11: 39S ribosomal protein L17, mitochondrial
+Macromolecule #12: Mitochondrial ribosomal protein L18, isoform CRA_b
+Macromolecule #13: 39S ribosomal protein L19, mitochondrial
+Macromolecule #14: 39S ribosomal protein L20, mitochondrial
+Macromolecule #15: 39S ribosomal protein L21, mitochondrial
+Macromolecule #16: 39S ribosomal protein L22, mitochondrial
+Macromolecule #17: 39S ribosomal protein L23, mitochondrial
+Macromolecule #18: 39S ribosomal protein L24, mitochondrial
+Macromolecule #19: 39S ribosomal protein L27, mitochondrial
+Macromolecule #20: 39S ribosomal protein L28, mitochondrial
+Macromolecule #21: 39S ribosomal protein L47, mitochondrial
+Macromolecule #22: 39S ribosomal protein L30, mitochondrial
+Macromolecule #23: 39S ribosomal protein L32, mitochondrial
+Macromolecule #24: 39S ribosomal protein L33, mitochondrial
+Macromolecule #25: 39S ribosomal protein L34, mitochondrial
+Macromolecule #26: 39S ribosomal protein L35, mitochondrial
+Macromolecule #27: 39S ribosomal protein L36, mitochondrial
+Macromolecule #28: 39S ribosomal protein L37, mitochondrial
+Macromolecule #29: 39S ribosomal protein L38, mitochondrial
+Macromolecule #30: 39S ribosomal protein L39, mitochondrial
+Macromolecule #31: 39S ribosomal protein L40, mitochondrial
+Macromolecule #32: 39S ribosomal protein L41, mitochondrial
+Macromolecule #33: 39S ribosomal protein L42, mitochondrial
+Macromolecule #34: 39S ribosomal protein L43, mitochondrial
+Macromolecule #35: 39S ribosomal protein L44, mitochondrial
+Macromolecule #36: 39S ribosomal protein L45, mitochondrial
+Macromolecule #37: 39S ribosomal protein L46, mitochondrial
+Macromolecule #38: 39S ribosomal protein L48, mitochondrial
+Macromolecule #39: 39S ribosomal protein L49, mitochondrial
+Macromolecule #40: 39S ribosomal protein L50, mitochondrial
+Macromolecule #41: 39S ribosomal protein L51, mitochondrial
+Macromolecule #42: cDNA FLJ76418, highly similar to Homo sapiens mitochondrial ribos...
+Macromolecule #43: 39S ribosomal protein L53, mitochondrial
+Macromolecule #44: 39S ribosomal protein L54, mitochondrial
+Macromolecule #45: 39S ribosomal protein L55, mitochondrial
+Macromolecule #46: Ribosomal protein 63, mitochondrial
+Macromolecule #47: Peptidyl-tRNA hydrolase ICT1, mitochondrial
+Macromolecule #48: Growth arrest and DNA damage-inducible proteins-interacting protein 1
+Macromolecule #49: 39S ribosomal protein S18a, mitochondrial
+Macromolecule #50: 39S ribosomal protein S30, mitochondrial
+Macromolecule #51: Unknown protein/protein extension
+Macromolecule #52: Mitochondrial assembly of ribosomal large subunit protein 1
+Macromolecule #53: MIEF1 upstream open reading frame protein
+Macromolecule #54: Acyl carrier protein, mitochondrial
+Macromolecule #55: 50S ribosomal protein L1
+Macromolecule #58: nascent chain
+Macromolecule #60: Unknown protein/protein extension
+Macromolecule #61: unknown protein/protein extension
+Macromolecule #56: 16S rRNA
+Macromolecule #57: mt-tRNAVal
+Macromolecule #59: mt-tRNA
+Macromolecule #62: MAGNESIUM ION
+Macromolecule #63: ZINC ION
+Macromolecule #64: CHLORIDE ION
+Macromolecule #65: SODIUM ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.4 mg/mL |
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| Buffer | pH: 7.4 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi


Homo sapiens (human)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria)
Authors
United Kingdom, 3 items
Citation
UCSF Chimera







































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