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Yorodumi- EMDB-15542: Human mitochondrial ribosome small subunit in complex with strept... -
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Open data
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Basic information
| Entry | ![]() | ||||||||||||||||||
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| Title | Human mitochondrial ribosome small subunit in complex with streptomycin | ||||||||||||||||||
Map data | SSU_body_masked_local_resolution_filtered | ||||||||||||||||||
Sample |
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| Biological species | Homo sapiens (human) | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.3 Å | ||||||||||||||||||
Authors | Singh V / Khawaja A / Itoh Y / Naschberger A / Rorbach J / Amunts A | ||||||||||||||||||
| Funding support | Sweden, European Union, 5 items
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Citation | Journal: Elife / Year: 2022Title: Structure of the mitoribosomal small subunit with streptomycin reveals Fe-S clusters and physiological molecules. Authors: Yuzuru Itoh / Vivek Singh / Anas Khawaja / Andreas Naschberger / Minh Duc Nguyen / Joanna Rorbach / Alexey Amunts / ![]() Abstract: The mitoribosome regulates cellular energy production, and its dysfunction is associated with aging. Inhibition of the mitoribosome can be caused by off-target binding of antimicrobial drugs and was ...The mitoribosome regulates cellular energy production, and its dysfunction is associated with aging. Inhibition of the mitoribosome can be caused by off-target binding of antimicrobial drugs and was shown to be coupled with a bilateral decreased visual acuity. Previously, we reported mitochondria-specific protein aspects of the mitoribosome, and in this article we present a 2.4-Å resolution structure of the small subunit in a complex with the anti-tuberculosis drug streptomycin that reveals roles of non-protein components. We found iron-sulfur clusters that are coordinated by different mitoribosomal proteins, nicotinamide adenine dinucleotide (NAD) associated with rRNA insertion, and posttranslational modifications. This is the first evidence of inter-protein coordination of iron-sulfur, and the finding of iron-sulfur clusters and NAD as fundamental building blocks of the mitoribosome directly links to mitochondrial disease and aging. We also report details of streptomycin interactions, suggesting that the mitoribosome-bound streptomycin is likely to be in hydrated gem-diol form and can be subjected to other modifications by the cellular milieu. The presented approach of adding antibiotics to cultured cells can be used to define their native structures in a bound form under more physiological conditions, and since streptomycin is a widely used drug for treatment, the newly resolved features can serve as determinants for targeting. | ||||||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_15542.map.gz | 241.6 MB | EMDB map data format | |
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| Header (meta data) | emd-15542-v30.xml emd-15542.xml | 14.8 KB 14.8 KB | Display Display | EMDB header |
| Images | emd_15542.png | 59.3 KB | ||
| Masks | emd_15542_msk_1.map | 421.9 MB | Mask map | |
| Others | emd_15542_additional_1.map.gz emd_15542_half_map_1.map.gz emd_15542_half_map_2.map.gz | 336.9 MB 339.1 MB 339.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15542 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15542 | HTTPS FTP |
-Validation report
| Summary document | emd_15542_validation.pdf.gz | 670.2 KB | Display | EMDB validaton report |
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| Full document | emd_15542_full_validation.pdf.gz | 669.8 KB | Display | |
| Data in XML | emd_15542_validation.xml.gz | 17.6 KB | Display | |
| Data in CIF | emd_15542_validation.cif.gz | 20.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15542 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15542 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_15542.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | SSU_body_masked_local_resolution_filtered | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_15542_msk_1.map | ||||||||||||
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-Additional map: #1
| File | emd_15542_additional_1.map | ||||||||||||
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-Half map: #1
| File | emd_15542_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_15542_half_map_2.map | ||||||||||||
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Sample components
-Entire : In vitro reconstituted complex of human mitochondrial ribosomal s...
| Entire | Name: In vitro reconstituted complex of human mitochondrial ribosomal small subunit and streptomycin |
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| Components |
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-Supramolecule #1: In vitro reconstituted complex of human mitochondrial ribosomal s...
| Supramolecule | Name: In vitro reconstituted complex of human mitochondrial ribosomal small subunit and streptomycin type: complex / ID: 1 / Chimera: Yes / Parent: 0 |
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| Source (natural) | Organism: Homo sapiens (human) |
-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: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.4 µm |
| Sample stage | Specimen holder model: SIDE ENTRY, EUCENTRIC / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 899952 |
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| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi



Homo sapiens (human)
Authors
Sweden, European Union, 5 items
Citation

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Y (Row.)
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FIELD EMISSION GUN
