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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | DalDro bound to the terminating Escherichia coli 70S ribosome | |||||||||
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Sample |
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Keywords | DalDro / Dal2 / Drosocin / PrAMP / Translation / Inhibitor / Termination / NCPET / Ribosome / Cryo-EM / ANTIBIOTIC | |||||||||
| Function / homology | Function and homology informationpositive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria / defense response to insect / translation release factor activity, codon specific / negative regulation of cytoplasmic translational initiation / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / response to bacterium ...positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria / defense response to insect / translation release factor activity, codon specific / negative regulation of cytoplasmic translational initiation / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / response to bacterium / translational termination / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / four-way junction DNA binding / negative regulation of cytoplasmic translation / regulation of mRNA stability / DnaA-L2 complex / translation repressor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / regulation of DNA-templated transcription elongation / response to reactive oxygen species / transcription elongation factor complex / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / transcription antitermination / DNA endonuclease activity / defense response / regulation of cell growth / translational initiation / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / transferase activity / antibacterial humoral response / ribosomal small subunit assembly / ribosome binding / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / defense response to Gram-negative bacterium / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / defense response to bacterium / negative regulation of translation / defense response to Gram-positive bacterium / rRNA binding / structural constituent of ribosome / ribosome / translation / innate immune response / response to antibiotic / negative regulation of DNA-templated transcription / hydrolase activity / mRNA binding / DNA binding / RNA binding / extracellular region / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.11 Å | |||||||||
Authors | Berger MJ / Safdari HA / Wilson DN | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome. Authors: Weiping Huang / Max J Berger / Haaris A Safdari / Dorota Klepacki / Helge Paternoga / Chetana Baliga / Daniel N Wilson / Nora Vázquez-Laslop / Alexander S Mankin / ![]() Abstract: Proline-rich antimicrobial peptides (PrAMPs) kill bacteria by binding in the ribosomal nascent peptide exit tunnel. Type II PrAMPs bind in an orientation matching that of the nascent protein, trap ...Proline-rich antimicrobial peptides (PrAMPs) kill bacteria by binding in the ribosomal nascent peptide exit tunnel. Type II PrAMPs bind in an orientation matching that of the nascent protein, trap the release factors and arrest ribosomes at stop codons. Conversely, Type I PrAMPs bind in an opposite orientation: their N-terminus invades the peptidyl transferase center arresting translation at start codons. Here, by mining the genome databases, we identify a number of PrAMPs with high sequence similarity to the Type II PrAMP Drosocin. Notably, many of the new PrAMPs do not stall ribosomes at stop codons, but act as Type I PrAMPs arresting translation at start codons. Structural analysis shows that such peptides bind with a Type I orientation. Minimal alterations in the peptide structure can flip the orientation of the PrAMP in the exit tunnel, switching the mechanism of translation inhibition. Altering the mode of binding and action of a PrAMP by only few mutations could be exploited by the host to combat newly emerging bacterial pathogens. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Header (meta data) | emd-55847-v30.xml emd-55847.xml | 75.4 KB 75.4 KB | Display Display | EMDB header |
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| FSC (resolution estimation) | emd_55847_fsc.xml | 14.7 KB | Display | FSC data file |
| Images | emd_55847.png | 53.7 KB | ||
| Map data | emd_55847.map.gz | 217.7 MB | EMDB map data format | |
| Masks | emd_55847_msk_1.map | 274.6 MB | Mask map | |
| Filedesc metadata | emd-55847.cif.gz | 14.6 KB | ||
| Others | emd_55847_additional_1.map.gz emd_55847_half_map_1.map.gz emd_55847_half_map_2.map.gz | 256.4 MB 219.1 MB 219.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55847 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55847 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9teyMC ![]() 9tewC ![]() 9texC ![]() 9tezC 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
-Supplemental data
-Mask #1
| File | emd_55847_msk_1.map | ||||||||||||
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-Additional map: #1
| File | emd_55847_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_55847_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_55847_half_map_2.map | ||||||||||||
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Sample components
+Entire : DalDro bound to the terminating 70S E. coli ribosome
+Supramolecule #1: DalDro bound to the terminating 70S E. coli ribosome
+Macromolecule #1: Large ribosomal subunit protein bL33
+Macromolecule #2: Large ribosomal subunit protein bL34
+Macromolecule #3: Large ribosomal subunit protein bL35
+Macromolecule #4: Large ribosomal subunit protein bL36A
+Macromolecule #5: Drosocin
+Macromolecule #6: 30S ribosomal protein S2
+Macromolecule #7: Small ribosomal subunit protein uS3
+Macromolecule #8: Small ribosomal subunit protein uS4
+Macromolecule #9: Small ribosomal subunit protein uS5
+Macromolecule #10: 30S ribosomal protein S6, fully modified isoform
+Macromolecule #11: 30S ribosomal protein S7
+Macromolecule #12: Small ribosomal subunit protein uS8
+Macromolecule #13: Small ribosomal subunit protein uS9
+Macromolecule #14: Small ribosomal subunit protein uS10
+Macromolecule #15: Small ribosomal subunit protein uS11
+Macromolecule #16: Small ribosomal subunit protein uS12
+Macromolecule #17: Small ribosomal subunit protein uS13
+Macromolecule #18: Small ribosomal subunit protein uS14
+Macromolecule #19: Small ribosomal subunit protein uS15
+Macromolecule #20: 30S ribosomal protein S16
+Macromolecule #21: Small ribosomal subunit protein uS17
+Macromolecule #22: Small ribosomal subunit protein bS18
+Macromolecule #23: Small ribosomal subunit protein uS19
+Macromolecule #24: 30S ribosomal protein S20
+Macromolecule #25: Small ribosomal subunit protein bS21
+Macromolecule #26: Peptide chain release factor RF1
+Macromolecule #29: Large ribosomal subunit protein uL2
+Macromolecule #30: Large ribosomal subunit protein uL3
+Macromolecule #31: Large ribosomal subunit protein uL4
+Macromolecule #32: Large ribosomal subunit protein uL5
+Macromolecule #33: Large ribosomal subunit protein uL6
+Macromolecule #34: Large ribosomal subunit protein bL9
+Macromolecule #35: Large ribosomal subunit protein uL13
+Macromolecule #36: Large ribosomal subunit protein uL14
+Macromolecule #37: 50S ribosomal protein L15
+Macromolecule #38: Large ribosomal subunit protein uL16
+Macromolecule #39: Large ribosomal subunit protein bL17
+Macromolecule #40: Large ribosomal subunit protein uL18
+Macromolecule #41: Large ribosomal subunit protein bL19
+Macromolecule #42: Large ribosomal subunit protein bL20
+Macromolecule #43: Large ribosomal subunit protein bL21
+Macromolecule #44: Large ribosomal subunit protein uL22
+Macromolecule #45: Large ribosomal subunit protein uL23
+Macromolecule #46: Large ribosomal subunit protein uL24
+Macromolecule #47: 50S ribosomal protein L25
+Macromolecule #48: Large ribosomal subunit protein bL27
+Macromolecule #49: Large ribosomal subunit protein bL28
+Macromolecule #50: Large ribosomal subunit protein uL29
+Macromolecule #51: Large ribosomal subunit protein uL30
+Macromolecule #52: Large ribosomal subunit protein bL32
+Macromolecule #53: Large ribosomal subunit protein bL31A
+Macromolecule #27: P-site Phe-tRNA
+Macromolecule #28: 5S rRNA
+Macromolecule #54: 23S rRNA
+Macromolecule #55: 16S rRNA
+Macromolecule #56: ZINC ION
+Macromolecule #57: SPERMINE
+Macromolecule #58: water
-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-PROPANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 1.14 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: 0.9 µm / Nominal defocus min: 0.3 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Germany, 1 items
Citation












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Processing
FIELD EMISSION GUN


