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Yorodumi- EMDB-3637: The cryo-EM structure of hibernating 100S ribosome dimer from pat... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-3637 | |||||||||
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Title | The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus | |||||||||
Map data | cryo-EM maps of S. aureus 100S complex (unsharpened) | |||||||||
Sample |
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Function / homology | Function and homology information large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / tRNA binding ...large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / zinc ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Staphylococcus aureus (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.76 Å | |||||||||
Authors | Matzov D / Aibara S / Zimmerman E / Bashan A / Amunts A / Yonath A | |||||||||
Citation | Journal: Nat Commun / Year: 2017 Title: The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus. Authors: Donna Matzov / Shintaro Aibara / Arnab Basu / Ella Zimmerman / Anat Bashan / Mee-Ngan F Yap / Alexey Amunts / Ada E Yonath / Abstract: Formation of 100S ribosome dimer is generally associated with translation suppression in bacteria. Trans-acting factors ribosome modulation factor (RMF) and hibernating promoting factor (HPF) were ...Formation of 100S ribosome dimer is generally associated with translation suppression in bacteria. Trans-acting factors ribosome modulation factor (RMF) and hibernating promoting factor (HPF) were shown to directly mediate this process in E. coli. Gram-positive S. aureus lacks an RMF homolog and the structural basis for its 100S formation was not known. Here we report the cryo-electron microscopy structure of the native 100S ribosome from S. aureus, revealing the molecular mechanism of its formation. The structure is distinct from previously reported analogs and relies on the HPF C-terminal extension forming the binding platform for the interactions between both of the small ribosomal subunits. The 100S dimer is formed through interactions between rRNA h26, h40, and protein uS2, involving conformational changes of the head as well as surface regions that could potentially prevent RNA polymerase from docking to the ribosome.Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation suppression by the ribosome-silencing factors. | |||||||||
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_3637.map.gz | 191.9 MB | EMDB map data format | |
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Header (meta data) | emd-3637-v30.xml emd-3637.xml | 84 KB 84 KB | Display Display | EMDB header |
Images | emd_3637.png | 49.7 KB | ||
Others | emd_3637_additional.map.gz emd_3637_half_map_1.map.gz emd_3637_half_map_2.map.gz | 211.7 MB 192.4 MB 192.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-3637 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-3637 | HTTPS FTP |
-Validation report
Summary document | emd_3637_validation.pdf.gz | 421.3 KB | Display | EMDB validaton report |
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Full document | emd_3637_full_validation.pdf.gz | 420.4 KB | Display | |
Data in XML | emd_3637_validation.xml.gz | 14.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-3637 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-3637 | HTTPS FTP |
-Related structure data
Related structure data | 6fxcMC 3640C 5ngmC M: atomic model generated by this map C: citing same article (ref.) |
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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_3637.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | cryo-EM maps of S. aureus 100S complex (unsharpened) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.605 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: ryo-EM maps of S. aureus 100S complex with...
File | emd_3637_additional.map | ||||||||||||
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Annotation | ryo-EM maps of S. aureus 100S complex with both large subunits masked out (unsharpened) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: First half map of the masked S. aureus 100S complex
File | emd_3637_half_map_1.map | ||||||||||||
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Annotation | First half map of the masked S. aureus 100S complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Second half map of the masked S. aureus 100S complex
File | emd_3637_half_map_2.map | ||||||||||||
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Annotation | Second half map of the masked S. aureus 100S complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 100S complex of Staphylococcus aureus
+Supramolecule #1: 100S complex of Staphylococcus aureus
+Supramolecule #2: 30S subunit
+Supramolecule #3: 50S subunit
+Supramolecule #4: 23S and 5S rRNA
+Supramolecule #5: 50S ribosomal proteins
+Supramolecule #6: 16S rRNA
+Supramolecule #7: 30S ribosomal proteins
+Macromolecule #1: 16S ribosomal RNA
+Macromolecule #23: 23S ribosomal RNA
+Macromolecule #24: 5S ribosomal RNA
+Macromolecule #2: 30S ribosomal protein S2
+Macromolecule #3: 30S ribosomal protein S3
+Macromolecule #4: 30S ribosomal protein S4
+Macromolecule #5: 30S ribosomal protein S5
+Macromolecule #6: 30S ribosomal protein S6
+Macromolecule #7: 30S ribosomal protein S7
+Macromolecule #8: 30S ribosomal protein S8
+Macromolecule #9: 30S ribosomal protein S9
+Macromolecule #10: 30S ribosomal protein S10
+Macromolecule #11: 30S ribosomal protein S11
+Macromolecule #12: 30S ribosomal protein S12
+Macromolecule #13: 30S ribosomal protein S13
+Macromolecule #14: 30S ribosomal protein S14 type Z
+Macromolecule #15: 30S ribosomal protein S15
+Macromolecule #16: 30S ribosomal protein S16
+Macromolecule #17: 30S ribosomal protein S17
+Macromolecule #18: 30S ribosomal protein S18
+Macromolecule #19: 30S ribosomal protein S19
+Macromolecule #20: 30S ribosomal protein S20
+Macromolecule #21: 30S ribosomal protein S21
+Macromolecule #22: Ribosome hibernation promotion factor
+Macromolecule #25: 50S ribosomal protein L2
+Macromolecule #26: 50S ribosomal protein L3
+Macromolecule #27: 50S ribosomal protein L4
+Macromolecule #28: 50S ribosomal protein L5
+Macromolecule #29: 50S ribosomal protein L6
+Macromolecule #30: 50S ribosomal protein L13
+Macromolecule #31: 50S ribosomal protein L14
+Macromolecule #32: 50S ribosomal protein L15
+Macromolecule #33: 50S ribosomal protein L16
+Macromolecule #34: 50S ribosomal protein L17
+Macromolecule #35: 50S ribosomal protein L18
+Macromolecule #36: 50S ribosomal protein L19
+Macromolecule #37: 50S ribosomal protein L20
+Macromolecule #38: 50S ribosomal protein L21
+Macromolecule #39: 50S ribosomal protein L22
+Macromolecule #40: 50S ribosomal protein L23
+Macromolecule #41: 50S ribosomal protein L24
+Macromolecule #42: 50S ribosomal protein L25
+Macromolecule #43: 50S ribosomal protein L27
+Macromolecule #44: 50S ribosomal protein L28
+Macromolecule #45: 50S ribosomal protein L29
+Macromolecule #46: 50S ribosomal protein L30
+Macromolecule #47: 50S ribosomal protein L31 type B
+Macromolecule #48: 50S ribosomal protein L32
+Macromolecule #49: 50S ribosomal protein L33
+Macromolecule #50: 50S ribosomal protein L34
+Macromolecule #51: 50S ribosomal protein L35
+Macromolecule #52: 50S ribosomal protein L36
-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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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 2.3 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Number classes used: 1 / Resolution.type: BY AUTHOR / Resolution: 6.76 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 12570 |
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Initial angle assignment | Type: OTHER |
Final angle assignment | Type: OTHER |