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Yorodumi- EMDB-45185: Cutibacterium acnes 50S ribosomal subunit with Clindamycin bound -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-45185 | |||||||||
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Title | Cutibacterium acnes 50S ribosomal subunit with Clindamycin bound | |||||||||
Map data | unsharpened map, flipped | |||||||||
Sample |
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Keywords | ribosome / clindamycin / acne / ANTIBIOTIC | |||||||||
Function / homology | Function and homology information large ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding ...large ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Cutibacterium acnes (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.53 Å | |||||||||
Authors | Lomakin IB / Devarkar SC / Bunick CG | |||||||||
Funding support | Canada, 1 items
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Citation | Journal: J Invest Dermatol / Year: 2024 Title: Mechanistic Basis for the Translation Inhibition of Cutibacterium acnes by Clindamycin. Authors: Ivan B Lomakin / Swapnil C Devarkar / Ayman Grada / Christopher G Bunick / Abstract: Inflammation and the Gram-positive anaerobic bacterium Cutibacterium acnes, which is implicated in acne pathogenesis and pilosebaceous-unit inflammation, are the main targets of antibiotic-based ...Inflammation and the Gram-positive anaerobic bacterium Cutibacterium acnes, which is implicated in acne pathogenesis and pilosebaceous-unit inflammation, are the main targets of antibiotic-based therapy against acne vulgaris (acne). The most widely used antibiotics in acne therapy are tetracyclines, macrolides, and lincosamides. Unfortunately, C. acnes bacteria over the past several decades have demonstrated increased resistance to these antibiotics, particularly to clindamycin. The precise knowledge of how antibiotics interact with their clinical target is needed to overcome this problem. Toward this goal, we determined the structure of clindamycin in complex with the ribosome of C. acnes at 2.53 Å resolution using cryogenic electron microscopy. The galactose sugar moiety of clindamycin interacts with nucleotides of the 23S ribosomal RNA directly or through a conserved network of water-mediated interactions. Its propyl pyrrolidinyl group interacts with the 23S ribosomal RNA through van der Waals forces. Clindamycin binding to the C. acnes ribosome interferes with both: proper orientation of the aminoacyl group of the A-site bound transfer RNA that is needed for peptide bond formation and with the extension of the nascent peptide. Our data are important for advancing the understanding of antibiotic resistance and development of narrow-spectrum antibacterial drugs, which is an urgent need for contemporary antibiotic stewardship. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_45185.map.gz | 226.7 MB | EMDB map data format | |
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Header (meta data) | emd-45185-v30.xml emd-45185.xml | 46.5 KB 46.5 KB | Display Display | EMDB header |
Images | emd_45185.png | 89.3 KB | ||
Filedesc metadata | emd-45185.cif.gz | 10.7 KB | ||
Others | emd_45185_half_map_1.map.gz emd_45185_half_map_2.map.gz | 622.4 MB 622.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-45185 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-45185 | HTTPS FTP |
-Validation report
Summary document | emd_45185_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_45185_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_45185_validation.xml.gz | 19.8 KB | Display | |
Data in CIF | emd_45185_validation.cif.gz | 22.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-45185 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-45185 | HTTPS FTP |
-Related structure data
Related structure data | 9c4gMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_45185.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | unsharpened map, flipped | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.868 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_45185_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_45185_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 50S subunit with Clindamycin bound
+Supramolecule #1: 50S subunit with Clindamycin bound
+Macromolecule #1: 50S ribosomal protein L2
+Macromolecule #2: 50S ribosomal protein L3
+Macromolecule #3: 50S ribosomal protein L4
+Macromolecule #4: 50S ribosomal protein L5
+Macromolecule #5: 50S ribosomal protein L6
+Macromolecule #6: 50S ribosomal protein L13
+Macromolecule #7: 50S ribosomal protein L14
+Macromolecule #8: 50S ribosomal protein L15
+Macromolecule #9: 50S ribosomal protein L16
+Macromolecule #10: Large ribosomal subunit protein bL17
+Macromolecule #11: 50S ribosomal protein L18
+Macromolecule #12: 50S ribosomal protein L19
+Macromolecule #13: 50S ribosomal protein L20
+Macromolecule #14: Large ribosomal subunit protein bL21
+Macromolecule #15: 50S ribosomal protein L22
+Macromolecule #16: 50S ribosomal protein L23
+Macromolecule #17: Large ribosomal subunit protein uL24
+Macromolecule #18: 50S ribosomal protein L25
+Macromolecule #19: 50S ribosomal protein L27
+Macromolecule #20: 50S ribosomal protein L28
+Macromolecule #21: 50S ribosomal protein L29
+Macromolecule #22: 50S ribosomal protein L30
+Macromolecule #23: 50S ribosomal protein L32
+Macromolecule #24: 50S ribosomal protein L33
+Macromolecule #25: 50S ribosomal protein L34
+Macromolecule #26: Large ribosomal subunit protein bL35
+Macromolecule #27: 50S ribosomal protein L31
+Macromolecule #30: 50S ribosomal protein bL37
+Macromolecule #31: 50S ribosomal protein L36
+Macromolecule #28: 23S rRNA
+Macromolecule #29: 5S rRNA
+Macromolecule #32: MAGNESIUM ION
+Macromolecule #33: ZINC ION
+Macromolecule #34: CLINDAMYCIN
+Macromolecule #35: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average exposure time: 1.8 sec. / Average electron dose: 38.58 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.5 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | PDB-9c4g: |