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Yorodumi- EMDB-51973: Pooled 50S subunit C_(L22)- precursor states supplemented with Ap... -
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Basic information
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| Title | Pooled 50S subunit C_(L22)- precursor states supplemented with Api137 - Canonical PET exit Api137 | |||||||||||||||
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Keywords | ribosome / antimicrobial peptide / RNA / ribosomal protein / PrAMP / proline-rich peptide / antibiotics / 50S / Api137 | |||||||||||||||
| Function / homology | Function and homology informationtranscriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translation repressor activity / mRNA regulatory element binding translation repressor activity / ribosome assembly / DNA-templated transcription termination / mRNA 5'-UTR binding / large ribosomal subunit ...transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translation repressor activity / mRNA regulatory element binding translation repressor activity / ribosome assembly / DNA-templated transcription termination / mRNA 5'-UTR binding / large ribosomal subunit / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / defense response to bacterium / structural constituent of ribosome / ribosome / translation / innate immune response / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / extracellular region / zinc ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||||||||
| Biological species | ![]() ![]() | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.17 Å | |||||||||||||||
Authors | Lauer S / Nikolay R / Spahn CMT | |||||||||||||||
| Funding support | Germany, 4 items
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Citation | Journal: Nat Commun / Year: 2025Title: The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding. Authors: Simon Malte Lauer / Jakob Gasse / Andor Krizsan / Maren Reepmeyer / Thiemo Sprink / Rainer Nikolay / Christian M T Spahn / Ralf Hoffmann / ![]() Abstract: The proline-rich antimicrobial designer peptide Api137 inhibits protein expression in bacteria by binding simultaneously to the ribosomal polypeptide exit tunnel and the release factor (RF), ...The proline-rich antimicrobial designer peptide Api137 inhibits protein expression in bacteria by binding simultaneously to the ribosomal polypeptide exit tunnel and the release factor (RF), depleting the cellular RF pool and leading to ribosomal arrest at stop codons. This study investigates the additional effect of Api137 on the assembly of ribosomes using an Escherichia coli reporter strain expressing one ribosomal protein per 30S and 50S subunit tagged with mCherry and EGFP, respectively. Separation of cellular extracts derived from cells exposed to Api137 in a sucrose gradient reveals elevated levels of partially assembled and not fully matured precursors of the 50S subunit (pre-50S). High-resolution structures obtained by cryogenic electron microscopy demonstrate that a large proportion of pre-50S states are missing up to five proteins (uL22, bL32, uL29, bL23, and uL16) and have misfolded helices in 23S rRNA domain IV. These data suggest a second mechanism for Api137, wherein it disrupts 50S subunit assembly by inducing the formation of misfolded precursor particles potentially incapable of evolving into active ribosomes, suggesting a bactericidal mechanism. | |||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_51973.map.gz | 51.7 MB | EMDB map data format | |
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| Header (meta data) | emd-51973-v30.xml emd-51973.xml | 32.5 KB 32.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51973_fsc.xml | 9.9 KB | Display | FSC data file |
| Images | emd_51973.png | 124.4 KB | ||
| Masks | emd_51973_msk_1.map | 103 MB | Mask map | |
| Filedesc metadata | emd-51973.cif.gz | 8.6 KB | ||
| Others | emd_51973_half_map_1.map.gz emd_51973_half_map_2.map.gz | 95.5 MB 95.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51973 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51973 | HTTPS FTP |
-Validation report
| Summary document | emd_51973_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_51973_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_51973_validation.xml.gz | 17.9 KB | Display | |
| Data in CIF | emd_51973_validation.cif.gz | 22.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51973 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51973 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ha1MC ![]() 9h3kC ![]() 9h3lC ![]() 9h3mC ![]() 9h3nC ![]() 9h3oC ![]() 9h3pC ![]() 9h3qC ![]() 9h3rC ![]() 9h3sC ![]() 9h3tC ![]() 9h3uC ![]() 9h3vC ![]() 9h3wC ![]() 9h3xC ![]() 9h3yC ![]() 9h3zC ![]() 9ha2C ![]() 9ha3C ![]() 9ha4C ![]() 9ha5C ![]() 9ha6C ![]() 9ha7C ![]() 9haiC ![]() 9halC ![]() 9hamC 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_51973.map.gz / Format: CCP4 / Size: 103 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: 1.332 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51973_msk_1.map | ||||||||||||
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-Half map: #2
| File | emd_51973_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_51973_half_map_2.map | ||||||||||||
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Sample components
+Entire : Pooled pre50S substates derived from Api137-treated cells supplem...
+Supramolecule #1: Pooled pre50S substates derived from Api137-treated cells supplem...
+Macromolecule #1: Large ribosomal subunit protein bL34
+Macromolecule #2: Large ribosomal subunit protein uL13
+Macromolecule #3: Large ribosomal subunit protein uL14
+Macromolecule #4: Large ribosomal subunit protein bL17
+Macromolecule #5: Large ribosomal subunit protein bL19
+Macromolecule #6: Large ribosomal subunit protein bL20
+Macromolecule #7: Large ribosomal subunit protein bL21
+Macromolecule #8: Large ribosomal subunit protein uL23
+Macromolecule #9: Large ribosomal subunit protein uL24
+Macromolecule #10: Large ribosomal subunit protein uL29
+Macromolecule #12: 50S ribosomal protein L3
+Macromolecule #13: Large ribosomal subunit protein uL4
+Macromolecule #14: Large ribosomal subunit protein uL15
+Macromolecule #15: Apidaecins type 137
+Macromolecule #11: 23S ribosomal RNA
-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: 7.6 |
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| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number real images: 2794 / Average exposure time: 1.2 sec. / Average electron dose: 46.2 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords

Authors
Germany, 4 items
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Processing
FIELD EMISSION GUN

