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Yorodumi- EMDB-29304: The structure of a 50S ribosomal subunit in the Lyme disease path... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-29304 | |||||||||
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Title | The structure of a 50S ribosomal subunit in the Lyme disease pathogen Borreliella burgdorferi | |||||||||
Map data | Borreliella burgdorferi 50S ribosomal subunit | |||||||||
Sample |
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Keywords | hibernating ribosome / bacterial / pathogen / 50S / translation / RIBOSOME | |||||||||
Function / homology | Function and homology information ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit ...ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / 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 / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Borreliella burgdorferi (Lyme disease spirochete) / Borreliella burgdorferi B31 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Sharma MR / Manjari SR / Agrawal EK / Keshavan P / Koripella RK / Majumdar S / Marcinkiewicz AL / Lin YP / Agrawal RK / Banavali NK | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2023 Title: The structure of a hibernating ribosome in a Lyme disease pathogen. Authors: Manjuli R Sharma / Swati R Manjari / Ekansh K Agrawal / Pooja Keshavan / Ravi K Koripella / Soneya Majumdar / Ashley L Marcinkiewicz / Yi-Pin Lin / Rajendra K Agrawal / Nilesh K Banavali / Abstract: The spirochete bacterial pathogen Borrelia (Borreliella) burgdorferi (Bbu) affects more than 10% of the world population and causes Lyme disease in about half a million people in the US annually. ...The spirochete bacterial pathogen Borrelia (Borreliella) burgdorferi (Bbu) affects more than 10% of the world population and causes Lyme disease in about half a million people in the US annually. Therapy for Lyme disease includes antibiotics that target the Bbu ribosome. Here we present the structure of the Bbu 70S ribosome obtained by single particle cryo-electron microscopy at 2.9 Å resolution, revealing a bound hibernation promotion factor protein and two genetically non-annotated ribosomal proteins bS22 and bL38. The ribosomal protein uL30 in Bbu has an N-terminal α-helical extension, partly resembling the mycobacterial bL37 protein, suggesting evolution of bL37 and a shorter uL30 from a longer uL30 protein. Its analogy to proteins uL30m and mL63 in mammalian mitochondrial ribosomes also suggests a plausible evolutionary pathway for expansion of protein content in mammalian mitochondrial ribosomes. Computational binding free energy predictions for antibiotics reflect subtle distinctions in antibiotic-binding sites in the Bbu ribosome. Discovery of these features in the Bbu ribosome may enable better ribosome-targeted antibiotic design for Lyme disease treatment. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_29304.map.gz | 173.9 MB | EMDB map data format | |
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Header (meta data) | emd-29304-v30.xml emd-29304.xml | 53.5 KB 53.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_29304_fsc.xml | 16.6 KB | Display | FSC data file |
Images | emd_29304.png | 94 KB | ||
Masks | emd_29304_msk_1.map | 347.6 MB | Mask map | |
Filedesc metadata | emd-29304.cif.gz | 11.3 KB | ||
Others | emd_29304_half_map_1.map.gz emd_29304_half_map_2.map.gz | 323 MB 323 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-29304 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-29304 | HTTPS FTP |
-Validation report
Summary document | emd_29304_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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Full document | emd_29304_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | emd_29304_validation.xml.gz | 24.1 KB | Display | |
Data in CIF | emd_29304_validation.cif.gz | 31.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-29304 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-29304 | HTTPS FTP |
-Related structure data
Related structure data | 8fmwMC 8fn2MC C: citing same article (ref.) M: atomic model generated by this map |
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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_29304.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Borreliella burgdorferi 50S ribosomal subunit | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0961 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_29304_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Borreliella burgdorferi 50S ribosomal subunit half map B
File | emd_29304_half_map_1.map | ||||||||||||
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Annotation | Borreliella burgdorferi 50S ribosomal subunit half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Borreliella burgdorferi 50S ribosomal subunit half map A
File | emd_29304_half_map_2.map | ||||||||||||
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Annotation | Borreliella burgdorferi 50S ribosomal subunit half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 50S ribosomal subunit
+Supramolecule #1: 50S ribosomal subunit
+Macromolecule #1: 23S ribosomal RNA
+Macromolecule #2: 5S ribosomal RNA
+Macromolecule #3: 50S ribosomal protein L2
+Macromolecule #4: 50S ribosomal protein L3
+Macromolecule #5: 50S ribosomal protein L4
+Macromolecule #6: 50S ribosomal protein L5
+Macromolecule #7: 50S ribosomal protein L6
+Macromolecule #8: 50S ribosomal protein L9
+Macromolecule #9: 50S ribosomal protein L10
+Macromolecule #10: 50S ribosomal protein L11
+Macromolecule #11: 50S ribosomal protein L13
+Macromolecule #12: 50S ribosomal protein L14
+Macromolecule #13: 50S ribosomal protein L15
+Macromolecule #14: 50S ribosomal protein L16
+Macromolecule #15: 50S ribosomal protein L17
+Macromolecule #16: 50S ribosomal protein L18
+Macromolecule #17: 50S ribosomal protein L19
+Macromolecule #18: 50S ribosomal protein L20
+Macromolecule #19: 50S ribosomal protein L21
+Macromolecule #20: 50S ribosomal protein L22
+Macromolecule #21: 50S ribosomal protein L23
+Macromolecule #22: 50S ribosomal protein L24
+Macromolecule #23: 50S ribosomal protein L25
+Macromolecule #24: 50S ribosomal protein L27
+Macromolecule #25: 50S ribosomal protein L28
+Macromolecule #26: 50S ribosomal protein L29
+Macromolecule #27: 50S ribosomal protein uL30
+Macromolecule #28: 50S ribosomal protein L31 type B
+Macromolecule #29: 50S ribosomal protein L32
+Macromolecule #30: 50S ribosomal protein L33
+Macromolecule #31: 50S ribosomal protein L34
+Macromolecule #32: 50S ribosomal protein L35
+Macromolecule #33: 50S ribosomal protein L36
+Macromolecule #34: 50S ribosomal protein bL38
+Macromolecule #35: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.25 mg/mL | ||||||||||||
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Buffer | pH: 7.5 Component:
Details: HMA-10 buffer | ||||||||||||
Grid | Model: Quantifoil / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 50 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Slit width: 30 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Digitization - Frames/image: 1-50 / Number grids imaged: 1 / Number real images: 4661 / Average exposure time: 10.0 sec. / Average electron dose: 67.527 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.001 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8200000000000001 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL / Overall B value: 2 / Target criteria: Cross-correlation coefficient |
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Output model | PDB-8fmw: PDB-8fn2: |