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Yorodumi- EMDB-55526: Staphylococcus aureus 70S initiation complex with a natural mRNA -
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Open data
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Basic information
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| Title | Staphylococcus aureus 70S initiation complex with a natural mRNA | |||||||||
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Keywords | Shine-Delgarno / anti Shine-Delgarno / translation initiation / Staphylococcus aureus. / RIBOSOME | |||||||||
| Function / homology | Function and homology informationlarge ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / ribosomal large subunit assembly / 5S rRNA binding / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding ...large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / ribosomal large subunit assembly / 5S rRNA binding / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.3 Å | |||||||||
Authors | Bahena Ceron R / Klaholz B / Marzi S | |||||||||
| Funding support | France, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Extended Shine-Dalgarno motifs govern translation initiation in Staphylococcus aureus. Authors: Maximilian P Kohl / Roberto Bahena-Ceron / Béatrice Chane-Woon-Ming / Maria Kompatscher / Matthias D Erlacher / Charles Barchet / Ottilie von Loeffelholz / Pascale Romby / Bruno P Klaholz / Stefano Marzi / ![]() Abstract: Regulation of translation initiation is central to bacterial adaptation, but species-specific mechanisms remain poorly understood. We present high-resolution mapping of translation start sites in ...Regulation of translation initiation is central to bacterial adaptation, but species-specific mechanisms remain poorly understood. We present high-resolution mapping of translation start sites in Staphylococcus aureus, revealing distinct features of initiation alongside numerous unannotated small ORFs. Our analysis, combined with cryo-EM of a native mRNA-ribosome complex, shows that S. aureus relies on extended, start codon proximal Shine-Dalgarno (SD) interactions, creating specificity against phylogenetically distant bacteria. Several natural S. aureus initiation sites are not correctly decoded by E. coli ribosomes. We identify new and conserved non-canonical start codons, whose regulatory initiation sites contain these characteristic extended SD sequence motifs. Finally, we characterize a novel example of uORF-mediated translational control in S. aureus, demonstrating that translation of a small leader peptide modulates expression of a key biofilm regulator. The described mechanism involves codon rarity, ribosome pausing, and arginine availability, linking nutrient sensing to biofilm formation in this major human pathogen. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_55526.map.gz | 415.2 MB | EMDB map data format | |
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| Header (meta data) | emd-55526-v30.xml emd-55526.xml | 69.1 KB 69.1 KB | Display Display | EMDB header |
| Images | emd_55526.png | 54.8 KB | ||
| Filedesc metadata | emd-55526.cif.gz | 13.6 KB | ||
| Others | emd_55526_half_map_1.map.gz emd_55526_half_map_2.map.gz | 765 MB 765 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55526 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55526 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9t4rMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_55526.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.729 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_55526_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_55526_half_map_2.map | ||||||||||||
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Sample components
+Entire : 70S ribosome initiation complex
+Supramolecule #1: 70S ribosome initiation complex
+Macromolecule #1: Large ribosomal subunit protein bL33B
+Macromolecule #3: Large ribosomal subunit protein bL34
+Macromolecule #5: Large ribosomal subunit protein bL35
+Macromolecule #7: Large ribosomal subunit protein bL36
+Macromolecule #9: Large ribosomal subunit protein bL31B
+Macromolecule #10: Large ribosomal subunit protein uL2
+Macromolecule #12: Large ribosomal subunit protein uL3
+Macromolecule #13: Small ribosomal subunit protein uS2
+Macromolecule #14: Large ribosomal subunit protein uL4
+Macromolecule #15: Small ribosomal subunit protein uS3
+Macromolecule #16: Large ribosomal subunit protein uL5
+Macromolecule #17: Small ribosomal subunit protein uS4
+Macromolecule #18: Large ribosomal subunit protein uL6
+Macromolecule #19: Small ribosomal subunit protein uS5
+Macromolecule #20: Small ribosomal subunit protein uS10
+Macromolecule #21: Small ribosomal subunit protein bS6
+Macromolecule #22: Large ribosomal subunit protein uL15
+Macromolecule #23: Small ribosomal subunit protein uS7
+Macromolecule #24: Large ribosomal subunit protein uL16
+Macromolecule #25: Small ribosomal subunit protein uS8
+Macromolecule #26: Large ribosomal subunit protein bL17
+Macromolecule #27: Small ribosomal subunit protein uS9
+Macromolecule #28: Large ribosomal subunit protein uL18
+Macromolecule #29: Large ribosomal subunit protein uL13
+Macromolecule #30: Large ribosomal subunit protein bL19
+Macromolecule #31: Small ribosomal subunit protein uS11
+Macromolecule #32: Large ribosomal subunit protein bL20
+Macromolecule #33: Small ribosomal subunit protein uS12
+Macromolecule #34: Large ribosomal subunit protein bL21
+Macromolecule #35: Small ribosomal subunit protein uS13
+Macromolecule #36: Large ribosomal subunit protein uL22
+Macromolecule #37: Small ribosomal subunit protein uS14B
+Macromolecule #38: Large ribosomal subunit protein uL23
+Macromolecule #39: Small ribosomal subunit protein uS15
+Macromolecule #40: Large ribosomal subunit protein uL24
+Macromolecule #41: Small ribosomal subunit protein bS16
+Macromolecule #42: Large ribosomal subunit protein bL25
+Macromolecule #43: Small ribosomal subunit protein uS17
+Macromolecule #44: Large ribosomal subunit protein bL27
+Macromolecule #45: Small ribosomal subunit protein bS18
+Macromolecule #46: Large ribosomal subunit protein bL28
+Macromolecule #47: Small ribosomal subunit protein uS19
+Macromolecule #48: Large ribosomal subunit protein uL29
+Macromolecule #49: Small ribosomal subunit protein bS20
+Macromolecule #50: Large ribosomal subunit protein uL30
+Macromolecule #51: Large ribosomal subunit protein uL14
+Macromolecule #52: Large ribosomal subunit protein bL32
+Macromolecule #2: aur mRNA
+Macromolecule #4: Methionine tRNA
+Macromolecule #6: 23S rRNA
+Macromolecule #8: 5S rRNA
+Macromolecule #11: 16S rRNA
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7 |
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| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Authors
France, 1 items
Citation








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Processing
FIELD EMISSION GUN

