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Open data
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Basic information
| Entry | Database: PDB / ID: 9tez | |||||||||||||||||||||||||||||||||
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| Title | DalDroS bound to the Escherichia coli 50S ribosomal subunit | |||||||||||||||||||||||||||||||||
Components |
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Keywords | ANTIBIOTIC / DalDroS / DalDro / Dal2 / Drosocin / PrAMP / Translation / Inhibitor / Termination / NCPET / Ribosome / Cryo-EM | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationtranslation release factor activity, codon specific / negative regulation of cytoplasmic translational initiation / transcriptional attenuation / translational termination / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translation repressor activity / negative regulation of DNA-templated DNA replication initiation ...translation release factor activity, codon specific / negative regulation of cytoplasmic translational initiation / transcriptional attenuation / translational termination / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / response to reactive oxygen species / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / regulation of cell growth / translational initiation / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosome binding / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | ![]() ![]() | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.88 Å | |||||||||||||||||||||||||||||||||
Authors | Berger, M.J. / Safdari, H.A. / Wilson, D.N. | |||||||||||||||||||||||||||||||||
| Funding support | Germany, 1items
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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. | |||||||||||||||||||||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9tez.cif.gz | 2.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9tez.ent.gz | 1.7 MB | Display | PDB format |
| PDBx/mmJSON format | 9tez.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/te/9tez ftp://data.pdbj.org/pub/pdb/validation_reports/te/9tez | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 55849MC ![]() 9tewC ![]() 9texC ![]() 9teyC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
+Large ribosomal subunit protein ... , 27 types, 27 molecules 3d4012cefghijmnopqrstvwxyzl
-RNA chain , 3 types, 3 molecules VbZ
| #4: RNA chain | Mass: 941811.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #10: RNA chain | Mass: 38790.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: RNA chain | Mass: 24485.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-50S ribosomal protein ... , 2 types, 2 molecules ku
| #18: Protein | Mass: 15008.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #27: Protein | Mass: 10713.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide / Protein , 2 types, 2 molecules 8W
| #5: Protein/peptide | Mass: 2300.620 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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| #9: Protein | Mass: 40573.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 3 types, 4 molecules 




| #35: Chemical | | #36: Chemical | ChemComp-SPM / | #37: Chemical | ChemComp-MG / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: DalDroS bound to the 50S E. coli ribosomal subunit / Type: RIBOSOME / Entity ID: #1-#34 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 900 nm / Nominal defocus min: 300 nm |
| Image recording | Electron dose: 1.14 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.88 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 202610 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | Resolution: 2.88→245.68 Å / Cor.coef. Fo:Fc: 0.908 / WRfactor Rwork: 0.331 / SU B: 13.317 / SU ML: 0.242 / Average fsc free: 0 / Average fsc overall: 0.8645 / Average fsc work: 0.8645 / ESU R: 0.347 Details: Hydrogens have been added in their riding positions
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| Solvent computation | Solvent model: NONE | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 72.788 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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