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Open data
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Basic information
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| Title | Membrane-associated human mitoribosome in complex with TACO1 | |||||||||
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Keywords | mitochondria / mitoribosome / inner membrane / RIBOSOME | |||||||||
| Function / homology | Function and homology informationnegative regulation of mitochondrial RNA catabolic process / Complex IV assembly / motor learning / mitochondrial protein quality control / Mitochondrial RNA degradation / protein insertion into mitochondrial inner membrane from matrix / negative regulation of oxidoreductase activity / mitochondrial ribosome binding / membrane insertase activity / mitochondrial RNA catabolic process ...negative regulation of mitochondrial RNA catabolic process / Complex IV assembly / motor learning / mitochondrial protein quality control / Mitochondrial RNA degradation / protein insertion into mitochondrial inner membrane from matrix / negative regulation of oxidoreductase activity / mitochondrial ribosome binding / membrane insertase activity / mitochondrial RNA catabolic process / regulation of mitochondrial translation / mitochondrial respiratory chain complex IV assembly / Complex I biogenesis / rRNA import into mitochondrion / mitochondrial transcription / mitochondrial translational termination / negative regulation of ATP-dependent activity / Mitochondrial ribosome-associated quality control / mitochondrial translational elongation / flagellated sperm motility / mitochondrial ribosome assembly / Mitochondrial translation elongation / translation release factor activity, codon nonspecific / Mitochondrial translation initiation / mitochondrial proton-transporting ATP synthase complex assembly / Mitochondrial translation termination / negative regulation of mitotic nuclear division / translation release factor activity / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / mitochondrial small ribosomal subunit / nuclear inner membrane / peptidyl-tRNA hydrolase activity / mitochondrial translation / mitochondrion transport along microtubule / apoptotic mitochondrial changes / nuclear outer membrane / mitochondrial nucleoid / mitochondrial respiratory chain complex I assembly / positive regulation of proteolysis / ribosomal small subunit binding / spermatid development / anatomical structure morphogenesis / mRNA transport / single fertilization / sperm flagellum / RNA processing / beta-tubulin binding / Mitochondrial protein degradation / acrosomal vesicle / rescue of stalled cytosolic ribosome / aerobic respiration / condensed nuclear chromosome / cellular response to leukemia inhibitory factor / mitochondrion organization / mRNA 3'-UTR binding / protein tetramerization / apoptotic signaling pathway / autophagy / mitochondrial membrane / fibrillar center / cell junction / single-stranded DNA binding / double-stranded RNA binding / regulation of translation / ribosomal small subunit assembly / 5S rRNA binding / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / endonuclease activity / nuclear membrane / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cytoskeleton / tRNA binding / cell population proliferation / mitochondrial inner membrane / negative regulation of translation / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / intracellular membrane-bounded organelle / protein domain specific binding / nucleotide binding / mRNA binding / apoptotic process / ubiquitin protein ligase binding / positive regulation of DNA-templated transcription / GTP binding / nucleolus / perinuclear region of cytoplasm / protein homodimerization activity Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.46 Å | |||||||||
Authors | Wang S / Xiong Y / Zhang Y | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural basis of TACO1-mediated efficient mitochondrial translation. Authors: Shuhui Wang / Michele Brischigliaro / Yuekang Zhang / Chunxiang Wu / Wei Zheng / Antoni Barrientos / Yong Xiong / ![]() Abstract: Translation elongation is a universally conserved step in protein synthesis, relying on elongation factors that engage the ribosomal L7/L12 stalk to mediate aminoacyl-tRNA delivery, accommodation, ...Translation elongation is a universally conserved step in protein synthesis, relying on elongation factors that engage the ribosomal L7/L12 stalk to mediate aminoacyl-tRNA delivery, accommodation, and ribosomal translocation. Using in organello cryo-electron microscopy, we reveal how the mitochondrial translation accelerator TACO1 promotes efficient elongation on human mitoribosomes. TACO1 binds the mitoribosomal region typically bound by elongation factor Tu (mtEF-Tu), bridging the large and small subunits via contacts with 16S rRNA, bL12m, A-site tRNA, and uS12m. While active throughout elongation, TACO1 is especially critical when translating polyproline motifs. Its absence prolongs mtEF-Tu residence in A/T states, causes persistent mitoribosomal stalling and premature subunit dissociation. Structural analyses indicate that TACO1 competes with mtEF-Tu for mitoribosome binding, stabilizes A-site tRNA, and enhances peptidyl transfer through a mechanism distinct from EF-P and eIF5A. These findings suggest that bacterial TACO1 orthologs may serve analogous roles, highlighting an evolutionarily conserved strategy for maintaining elongation efficiency during challenging translation events. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_70592.map.gz | 18.1 MB | EMDB map data format | |
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| Header (meta data) | emd-70592-v30.xml emd-70592.xml | 144.7 KB 144.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_70592_fsc_1.xml emd_70592_fsc_2.xml emd_70592_fsc_3.xml | 15.7 KB 15.8 KB 15.7 KB | Display Display Display | FSC data file |
| Images | emd_70592.png | 73.3 KB | ||
| Masks | emd_70592_msk_1.map | 421.9 MB | Mask map | |
| Filedesc metadata | emd-70592.cif.gz | 25.3 KB | ||
| Others | emd_70592_additional_1.map.gz emd_70592_additional_10.map.gz emd_70592_additional_2.map.gz emd_70592_additional_3.map.gz emd_70592_additional_4.map.gz emd_70592_additional_5.map.gz emd_70592_additional_6.map.gz emd_70592_additional_7.map.gz emd_70592_additional_8.map.gz emd_70592_additional_9.map.gz emd_70592_half_map_1.map.gz emd_70592_half_map_2.map.gz | 213.1 MB 3.3 MB 391.9 MB 391.9 MB 398.9 MB 1.1 MB 213.5 MB 391.9 MB 391.9 MB 398.9 MB 392 MB 392 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70592 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70592 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9olfMC ![]() 9pr4C ![]() 9praC ![]() 9prdC ![]() 9prqC ![]() 9prxC ![]() 9ps0C ![]() 9ps7C ![]() 9psiC ![]() 9psmC ![]() 70619 C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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_70592.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.068 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
+Mask #1
+Additional map: #10
+Additional map: #1
+Additional map: #9
+Additional map: #8
+Additional map: #7
+Additional map: #6
+Additional map: #5
+Additional map: #4
+Additional map: #3
+Additional map: #2
+Half map: #2
+Half map: #1
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Sample components
+Entire : mitochondria
+Supramolecule #1: mitochondria
+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 #12: Small ribosomal subunit protein mS34
+Macromolecule #13: 28S ribosomal protein S35, mitochondrial
+Macromolecule #14: Small ribosomal subunit protein mS37
+Macromolecule #15: Aurora kinase A-interacting protein
+Macromolecule #16: Pentatricopeptide repeat domain-containing protein 3, mitochondrial
+Macromolecule #17: Leucine-rich PPR motif-containing protein, mitochondrial
+Macromolecule #18: SRA stem-loop-interacting RNA-binding protein, mitochondrial
+Macromolecule #20: 28S ribosomal protein S2, mitochondrial
+Macromolecule #21: 28S ribosomal protein S24, mitochondrial
+Macromolecule #22: 28S ribosomal protein S5, mitochondrial
+Macromolecule #23: 28S ribosomal protein S6, mitochondrial
+Macromolecule #24: 28S ribosomal protein S7, mitochondrial
+Macromolecule #25: 28S ribosomal protein S9, mitochondrial
+Macromolecule #26: 28S ribosomal protein S10, mitochondrial
+Macromolecule #27: 28S ribosomal protein S11, mitochondrial
+Macromolecule #28: 28S ribosomal protein S12, mitochondrial
+Macromolecule #29: 28S ribosomal protein S14, mitochondrial
+Macromolecule #30: 28S ribosomal protein S15, mitochondrial
+Macromolecule #31: 28S ribosomal protein S16, mitochondrial
+Macromolecule #32: 28S ribosomal protein S17, mitochondrial
+Macromolecule #33: 28S ribosomal protein S18b, mitochondrial
+Macromolecule #34: 28S ribosomal protein S18c, mitochondrial
+Macromolecule #35: Small ribosomal subunit protein bS21m
+Macromolecule #36: 28S ribosomal protein S22, mitochondrial
+Macromolecule #37: 28S ribosomal protein S23, mitochondrial
+Macromolecule #38: 28S ribosomal protein S25, mitochondrial
+Macromolecule #39: 28S ribosomal protein S26, mitochondrial
+Macromolecule #40: 28S ribosomal protein S27, mitochondrial
+Macromolecule #41: 28S ribosomal protein S28, mitochondrial
+Macromolecule #42: 28S ribosomal protein S29, mitochondrial
+Macromolecule #43: 28S ribosomal protein S31, mitochondrial
+Macromolecule #44: 28S ribosomal protein S33, mitochondrial
+Macromolecule #50: Translational activator of cytochrome c oxidase 1
+Macromolecule #51: 39S ribosomal protein L2, mitochondrial
+Macromolecule #52: 39S ribosomal protein L3, mitochondrial
+Macromolecule #53: 39S ribosomal protein L4, mitochondrial
+Macromolecule #54: 39S ribosomal protein L12, mitochondrial
+Macromolecule #55: 39S ribosomal protein L9, mitochondrial
+Macromolecule #56: 39S ribosomal protein L10, mitochondrial
+Macromolecule #57: 39S ribosomal protein L11, mitochondrial
+Macromolecule #58: Large ribosomal subunit protein uL13m
+Macromolecule #59: 39S ribosomal protein L14, mitochondrial
+Macromolecule #60: 39S ribosomal protein L15, mitochondrial
+Macromolecule #61: 39S ribosomal protein L16, mitochondrial
+Macromolecule #62: 39S ribosomal protein L17, mitochondrial
+Macromolecule #63: Mitochondrial inner membrane protein OXA1L
+Macromolecule #64: 39S ribosomal protein L18, mitochondrial
+Macromolecule #65: 39S ribosomal protein L19, mitochondrial
+Macromolecule #66: 39S ribosomal protein L20, mitochondrial
+Macromolecule #67: 39S ribosomal protein L21, mitochondrial
+Macromolecule #68: 39S ribosomal protein L22, mitochondrial
+Macromolecule #69: 39S ribosomal protein L23, mitochondrial
+Macromolecule #70: 39S ribosomal protein L24, mitochondrial
+Macromolecule #71: 39S ribosomal protein L27, mitochondrial
+Macromolecule #72: 39S ribosomal protein L28, mitochondrial
+Macromolecule #73: 39S ribosomal protein L47, mitochondrial
+Macromolecule #74: 39S ribosomal protein L30, mitochondrial
+Macromolecule #75: 39S ribosomal protein L42, mitochondrial
+Macromolecule #76: 39S ribosomal protein L43, mitochondrial
+Macromolecule #77: 39S ribosomal protein L44, mitochondrial
+Macromolecule #78: 39S ribosomal protein L45, mitochondrial
+Macromolecule #79: 39S ribosomal protein L46, mitochondrial
+Macromolecule #80: 39S ribosomal protein L48, mitochondrial
+Macromolecule #81: 39S ribosomal protein L49, mitochondrial
+Macromolecule #82: 39S ribosomal protein L50, mitochondrial
+Macromolecule #83: 39S ribosomal protein L51, mitochondrial
+Macromolecule #84: 39S ribosomal protein L52, mitochondrial
+Macromolecule #85: Large ribosomal subunit protein mL53
+Macromolecule #86: 39S ribosomal protein L54, mitochondrial
+Macromolecule #87: 39S ribosomal protein L55, mitochondrial
+Macromolecule #88: Nascent polypeptide
+Macromolecule #89: Ribosomal protein 63, mitochondrial
+Macromolecule #90: Peptidyl-tRNA hydrolase ICT1, mitochondrial
+Macromolecule #91: Growth arrest and DNA damage-inducible proteins-interacting protein 1
+Macromolecule #92: 39S ribosomal protein S18a, mitochondrial
+Macromolecule #93: 39S ribosomal protein S30, mitochondrial
+Macromolecule #94: Large ribosomal subunit protein uL1m
+Macromolecule #11: 16S mitochondrial rRNA
+Macromolecule #19: 12S mitochondrial rRNA
+Macromolecule #45: A/A-tRNA
+Macromolecule #46: P/P-tRNA
+Macromolecule #47: E/E-tRNA
+Macromolecule #48: mRNA
+Macromolecule #49: RNA (73-MER)mitochondrial tRNAVal
+Macromolecule #95: ZINC ION
+Macromolecule #96: SPERMIDINE
+Macromolecule #97: MAGNESIUM ION
+Macromolecule #98: 1,4-DIAMINOBUTANE
+Macromolecule #99: POTASSIUM ION
+Macromolecule #100: SPERMINE
+Macromolecule #101: NICOTINAMIDE-ADENINE-DINUCLEOTIDE
+Macromolecule #102: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #103: GUANOSINE-5'-DIPHOSPHATE
+Macromolecule #104: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #105: VALINE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | 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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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 55.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
United States, 1 items
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Processing
FIELD EMISSION GUN


