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Open data
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Basic information
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Title | Tetracycline bound to the 30S head | ||||||||||||
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![]() | Antibiotic / RIBOSOME | ||||||||||||
Function / homology | ![]() transcription antitermination factor activity, RNA binding / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / maintenance of translational fidelity / ribosome biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / cytoplasmic translation ...transcription antitermination factor activity, RNA binding / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / maintenance of translational fidelity / ribosome biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / cytoplasmic translation / tRNA binding / rRNA binding / negative regulation of translation / ribosome / structural constituent of ribosome / translation / response to antibiotic / mRNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 1.82 Å | ||||||||||||
![]() | Paternoga H / Crowe-McAuliffe C / Beckert B / Wilson DN | ||||||||||||
Funding support | European Union, 3 items
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![]() | ![]() Title: Structural conservation of antibiotic interaction with ribosomes. Authors: Helge Paternoga / Caillan Crowe-McAuliffe / Lars V Bock / Timm O Koller / Martino Morici / Bertrand Beckert / Alexander G Myasnikov / Helmut Grubmüller / Jiří Nováček / Daniel N Wilson / ![]() ![]() ![]() Abstract: The ribosome is a major target for clinically used antibiotics, but multidrug resistant pathogenic bacteria are making our current arsenal of antimicrobials obsolete. Here we present cryo-electron- ...The ribosome is a major target for clinically used antibiotics, but multidrug resistant pathogenic bacteria are making our current arsenal of antimicrobials obsolete. Here we present cryo-electron-microscopy structures of 17 distinct compounds from six different antibiotic classes bound to the bacterial ribosome at resolutions ranging from 1.6 to 2.2 Å. The improved resolution enables a precise description of antibiotic-ribosome interactions, encompassing solvent networks that mediate multiple additional interactions between the drugs and their target. Our results reveal a high structural conservation in the binding mode between antibiotics with the same scaffold, including ordered water molecules. Water molecules are visualized within the antibiotic binding sites that are preordered, become ordered in the presence of the drug and that are physically displaced on drug binding. Insight into RNA-ligand interactions will facilitate development of new antimicrobial agents, as well as other RNA-targeting therapies. | ||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 68.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 33.7 KB 33.7 KB | Display Display | ![]() |
Images | ![]() | 84.9 KB | ||
Filedesc metadata | ![]() | 8.3 KB | ||
Others | ![]() ![]() ![]() | 1.7 GB 1.6 GB 1.6 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8cf1MC ![]() 8ca7C ![]() 8caiC ![]() 8camC ![]() 8cazC ![]() 8cepC ![]() 8ceuC ![]() 8cf8C ![]() 8cgdC ![]() 8cgiC ![]() 8cgjC ![]() 8cgkC ![]() 8cgrC ![]() 8cguC ![]() 8cgvC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.681 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
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Density Histograms |
-Half map: #2
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Density Histograms |
-Half map: #1
File | emd_16615_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : 70S ribosomes with antibiotic cocktail
+Supramolecule #1: 70S ribosomes with antibiotic cocktail
+Macromolecule #1: 16S rRNA
+Macromolecule #2: 30S ribosomal protein S2
+Macromolecule #3: Small ribosomal subunit protein uS3
+Macromolecule #4: Small ribosomal subunit protein uS5
+Macromolecule #5: 30S ribosomal protein S7
+Macromolecule #6: Small ribosomal subunit protein uS9
+Macromolecule #7: Small ribosomal subunit protein uS10
+Macromolecule #8: Small ribosomal subunit protein uS13
+Macromolecule #9: Small ribosomal subunit protein uS14
+Macromolecule #10: Small ribosomal subunit protein uS19
+Macromolecule #11: TETRACYCLINE
+Macromolecule #12: MAGNESIUM ION
+Macromolecule #13: POTASSIUM ION
+Macromolecule #14: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GRAPHENE | |||||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Detector mode: COUNTING / Average exposure time: 4.5 sec. / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.0 µm / Nominal defocus min: 0.4 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 1.82 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 419159 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |