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Yorodumi- EMDB-3751: Cryo-EM reconstruction of the Mycobacterium smegmatis 70S ribosome -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-3751 | |||||||||
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Title | Cryo-EM reconstruction of the Mycobacterium smegmatis 70S ribosome | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information large ribosomal subunit rRNA binding / large ribosomal subunit / small ribosomal subunit / 5S rRNA binding / transferase activity / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / translation ...large ribosomal subunit rRNA binding / large ribosomal subunit / small ribosomal subunit / 5S rRNA binding / transferase activity / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / zinc ion binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Mycobacterium smegmatis str. MC2 155 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.31 Å | |||||||||
Authors | Hentschel J / Burnside C / Mignot I / Leibundgut M / Boehringer D / Ban N | |||||||||
Citation | Journal: Cell Rep / Year: 2017 Title: The Complete Structure of the Mycobacterium smegmatis 70S Ribosome. Authors: Jendrik Hentschel / Chloe Burnside / Ingrid Mignot / Marc Leibundgut / Daniel Boehringer / Nenad Ban / Abstract: The ribosome carries out the synthesis of proteins in every living cell. It consequently represents a frontline target in anti-microbial therapy. Tuberculosis ranks among the leading causes of death ...The ribosome carries out the synthesis of proteins in every living cell. It consequently represents a frontline target in anti-microbial therapy. Tuberculosis ranks among the leading causes of death worldwide, due in large part to the combination of difficult-to-treat latency and antibiotic resistance. Here, we present the 3.3-Å cryo-EM structure of the 70S ribosome of Mycobacterium smegmatis, a close relative to the human pathogen Mycobacterium tuberculosis. The structure reveals two additional ribosomal proteins and localizes them to the vicinity of drug-target sites in both the catalytic center and the decoding site of the ribosome. Furthermore, we visualized actinobacterium-specific rRNA and protein expansions that extensively remodel the ribosomal surface with implications for polysome organization. Our results provide a foundation for understanding the idiosyncrasies of mycobacterial translation and reveal atomic details of the structure that will facilitate the design of anti-tubercular therapeutics. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_3751.map.gz | 35.8 MB | EMDB map data format | |
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Header (meta data) | emd-3751-v30.xml emd-3751.xml | 66.8 KB 66.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_3751_fsc.xml | 10.1 KB | Display | FSC data file |
Images | emd_3751.png | 278.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-3751 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-3751 | HTTPS FTP |
-Related structure data
Related structure data | 5o61MC 3748C 3750C 5o5jC 5o60C C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_3751.map.gz / Format: CCP4 / Size: 38.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.39 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : 70S ribosome
+Supramolecule #1: 70S ribosome
+Macromolecule #1: 50S ribosomal protein bL37
+Macromolecule #4: 50S ribosomal protein L2
+Macromolecule #5: 50S ribosomal protein L3
+Macromolecule #6: 50S ribosomal protein L4
+Macromolecule #7: 50S ribosomal protein L5
+Macromolecule #8: 50S ribosomal protein L6
+Macromolecule #9: 50S ribosomal protein L9
+Macromolecule #10: 50S ribosomal protein L10
+Macromolecule #11: 50S ribosomal protein L11
+Macromolecule #12: 50S ribosomal protein L13
+Macromolecule #13: 50S ribosomal protein L14
+Macromolecule #14: 50S ribosomal protein L15
+Macromolecule #15: 50S ribosomal protein L16
+Macromolecule #16: 50S ribosomal protein L17
+Macromolecule #17: 50S ribosomal protein L18
+Macromolecule #18: 50S ribosomal protein L19
+Macromolecule #19: 50S ribosomal protein L20
+Macromolecule #20: 50S ribosomal protein L21
+Macromolecule #21: 50S ribosomal protein L22
+Macromolecule #22: 50S ribosomal protein L23
+Macromolecule #23: 50S ribosomal protein L24
+Macromolecule #24: 50S ribosomal protein L25
+Macromolecule #25: 50S ribosomal protein L27
+Macromolecule #26: LSU ribosomal protein L28P
+Macromolecule #27: 50S ribosomal protein L29
+Macromolecule #28: 50S ribosomal protein L30
+Macromolecule #29: 50S ribosomal protein L32
+Macromolecule #30: 50S ribosomal protein L33 1
+Macromolecule #31: 50S ribosomal protein L34
+Macromolecule #32: 50S ribosomal protein L35
+Macromolecule #33: 50S ribosomal protein L36
+Macromolecule #34: 50S ribosomal protein L31
+Macromolecule #36: Conserved domain protein
+Macromolecule #37: 30S ribosomal protein S3
+Macromolecule #38: 30S ribosomal protein S4
+Macromolecule #39: 30S ribosomal protein S5
+Macromolecule #40: 30S ribosomal protein S6
+Macromolecule #41: 30S ribosomal protein S7
+Macromolecule #42: 30S ribosomal protein S8
+Macromolecule #43: 30S ribosomal protein S9
+Macromolecule #44: 30S ribosomal protein S10
+Macromolecule #45: 30S ribosomal protein S11
+Macromolecule #46: 30S ribosomal protein S12
+Macromolecule #47: 30S ribosomal protein S13
+Macromolecule #48: 30S ribosomal protein S14 type Z
+Macromolecule #49: 30S ribosomal protein S15
+Macromolecule #50: 30S ribosomal protein S16
+Macromolecule #51: 30S ribosomal protein S17
+Macromolecule #52: 30S ribosomal protein S18 2
+Macromolecule #53: 30S ribosomal protein S19
+Macromolecule #54: 30S ribosomal protein S20
+Macromolecule #55: 30S ribosomal protein S2
+Macromolecule #2: 23S rRNA
+Macromolecule #3: 5S rRNA
+Macromolecule #35: 16S rRNA
+Macromolecule #56: P/P-site Phe-tRNA(Phe)
+Macromolecule #57: mRNA fragment
+Macromolecule #58: MAGNESIUM ION
+Macromolecule #59: ZINC ION
+Macromolecule #60: PHENYLALANINE
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER |
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 96 % / Instrument: FEI VITROBOT MARK I |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated magnification: 100719 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 20.0 e/Å2 / Details: FEI EPU data collection |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Protocol: OTHER |
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Output model | PDB-5o61: |