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Yorodumi- EMDB-51876: Assembly intermediate of human mitochondrial ribosome small subun... -
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Basic information
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| Title | Assembly intermediate of human mitochondrial ribosome small subunit in complex with NOA1 and partial RBFA (state N2) | |||||||||
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Keywords | mitochondria / small subunit / assembly / NOA1 / RIBOSOME | |||||||||
| Function / homology | Function and homology informationmitochondrial small ribosomal subunit assembly / RNA folding chaperone / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / mitochondrial ribosome / mitochondrial small ribosomal subunit / mitochondrial translation ...mitochondrial small ribosomal subunit assembly / RNA folding chaperone / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / mitochondrial ribosome / mitochondrial small ribosomal subunit / mitochondrial translation / ribosomal small subunit binding / Mitochondrial protein degradation / apoptotic signaling pathway / mitochondrion organization / cell population proliferation / rRNA processing / regulation of translation / small ribosomal subunit / small ribosomal subunit rRNA binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / tRNA binding / mitochondrial inner membrane / rRNA binding / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / mRNA binding / GTPase activity / apoptotic process / GTP binding / mitochondrion / RNA binding / nucleoplasm / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Singh V / Shiriaev D / Khawaja A / Rorbach J | |||||||||
| Funding support | Sweden, 2 items
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Citation | Journal: Nat Commun / Year: 2026Title: Pseudouridine synthase PUS1 and initiation factor mtIF2 are human mitoribosomal small subunit assembly factors. Authors: Vivek Singh / Dmitrii Shiriaev / Lorina Bilalli / Anas Khawaja / Joanna Rorbach / ![]() Abstract: Assembly of the mitochondrial ribosome (mitoribosome) is a crucial step in mitochondrial gene expression. This process facilitates mitochondrial translation, which produces essential subunits of the ...Assembly of the mitochondrial ribosome (mitoribosome) is a crucial step in mitochondrial gene expression. This process facilitates mitochondrial translation, which produces essential subunits of the oxidative phosphorylation machinery-the cell's primary energy-producing machinery. Disruptions in mitoribosome assembly can lead to severe human diseases. Given its fundamental importance, detailed structural analysis of mitoribosome assembly pathways is essential for advancing our understanding of mitochondrial function in both health and disease. In this study, we characterize twelve distinct assembly states of the mitoribosomal small subunit (mtSSU) isolated from human cells. Our findings reveal the intricate details of the final maturation stages of the mtSSU platform, decoding center, and the 3'-end of 12S rRNA. This process is governed by coordinated actions of assembly factors that ensure precise, stepwise rRNA folding and the integration of mitoribosomal proteins into the developing subunit. Our approach identifies pseudouridine synthase PUS1 and initiation factor mtIF2 as assembly factors, expanding their known roles beyond mt-tRNA maturation and translation, respectively. In addition, the identified assembly intermediates provide insight into the modular nature of mtSSU biogenesis in mitochondria and further link late-stage assembly to the acquisition of translational competence. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_51876.map.gz | 670.2 MB | EMDB map data format | |
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| Header (meta data) | emd-51876-v30.xml emd-51876.xml | 62.2 KB 62.2 KB | Display Display | EMDB header |
| Images | emd_51876.png | 74.2 KB | ||
| Filedesc metadata | emd-51876.cif.gz | 14 KB | ||
| Others | emd_51876_additional_1.map.gz emd_51876_half_map_1.map.gz emd_51876_half_map_2.map.gz | 721.4 MB 670.4 MB 670 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51876 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51876 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9h54MC ![]() 9h51C ![]() 9h52C ![]() 9h55C ![]() 9rorC ![]() 9rotC ![]() 9rovC ![]() 9rpfC M: atomic model generated by this map C: citing same article ( |
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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_51876.map.gz / Format: CCP4 / Size: 824 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: 1.01 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_51876_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_51876_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_51876_half_map_2.map | ||||||||||||
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Sample components
+Entire : mitoribosomal small subunit assembly intermediate
+Supramolecule #1: mitoribosomal small subunit assembly intermediate
+Macromolecule #1: 12S mitochondrial rRNA
+Macromolecule #2: 28S ribosomal protein S2, mitochondrial
+Macromolecule #3: 28S ribosomal protein S24, mitochondrial
+Macromolecule #4: 28S ribosomal protein S5, mitochondrial
+Macromolecule #5: 28S ribosomal protein S6, mitochondrial
+Macromolecule #6: 28S ribosomal protein S7, mitochondrial
+Macromolecule #7: 28S ribosomal protein S9, mitochondrial
+Macromolecule #8: 28S ribosomal protein S10, mitochondrial
+Macromolecule #9: 28S ribosomal protein S11, mitochondrial
+Macromolecule #10: 28S ribosomal protein S12, mitochondrial
+Macromolecule #11: 28S ribosomal protein S14, mitochondrial
+Macromolecule #12: 28S ribosomal protein S15, mitochondrial
+Macromolecule #13: 28S ribosomal protein S16, mitochondrial
+Macromolecule #14: 28S ribosomal protein S17, mitochondrial
+Macromolecule #15: 28S ribosomal protein S18b, mitochondrial
+Macromolecule #16: 28S ribosomal protein S18c, mitochondrial
+Macromolecule #17: Small ribosomal subunit protein bS21m
+Macromolecule #18: 28S ribosomal protein S22, mitochondrial
+Macromolecule #19: 28S ribosomal protein S23, mitochondrial
+Macromolecule #20: 28S ribosomal protein S25, mitochondrial
+Macromolecule #21: 28S ribosomal protein S26, mitochondrial
+Macromolecule #22: 28S ribosomal protein S27, mitochondrial
+Macromolecule #23: 28S ribosomal protein S28, mitochondrial
+Macromolecule #24: 28S ribosomal protein S29, mitochondrial
+Macromolecule #25: 28S ribosomal protein S31, mitochondrial
+Macromolecule #26: 28S ribosomal protein S33, mitochondrial
+Macromolecule #27: Small ribosomal subunit protein mS34
+Macromolecule #28: 28S ribosomal protein S35, mitochondrial
+Macromolecule #29: Pentatricopeptide repeat domain-containing protein 3, mitochondrial
+Macromolecule #30: Nitric oxide-associated protein 1
+Macromolecule #31: Putative ribosome-binding factor A, mitochondrial
+Macromolecule #32: MAGNESIUM ION
+Macromolecule #33: POTASSIUM ION
+Macromolecule #34: ZINC ION
+Macromolecule #35: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #36: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #37: GUANOSINE-5'-DIPHOSPHATE
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 45.0 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: 1.8 µm / Nominal defocus min: 0.4 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Sweden, 2 items
Citation






















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Processing
FIELD EMISSION GUN

