+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-13191 | |||||||||
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Title | Staphylococcus aureus ribosome in complex with Sal(B) | |||||||||
Map data | consensus map | |||||||||
Sample |
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Function / homology | Function and homology information large ribosomal subunit / 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 ...large ribosomal subunit / 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) / Staphylococcus lentus (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Nicholson D / Ranson NA / O'Neill AJ | |||||||||
Funding support | United Kingdom, 1 items
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Citation | Journal: Nucleic Acids Res / Year: 2022 Title: Sal-type ABC-F proteins: intrinsic and common mediators of pleuromutilin resistance by target protection in staphylococci. Authors: Merianne Mohamad / David Nicholson / Chayan Kumar Saha / Vasili Hauryliuk / Thomas A Edwards / Gemma C Atkinson / Neil A Ranson / Alex J O'Neill / Abstract: The first member of the pleuromutilin (PLM) class suitable for systemic antibacterial chemotherapy in humans recently entered clinical use, underscoring the need to better understand mechanisms of ...The first member of the pleuromutilin (PLM) class suitable for systemic antibacterial chemotherapy in humans recently entered clinical use, underscoring the need to better understand mechanisms of PLM resistance in disease-causing bacterial genera. Of the proteins reported to mediate PLM resistance in staphylococci, the least-well studied to date is Sal(A), a putative ABC-F NTPase that-by analogy to other proteins of this type-may act to protect the ribosome from PLMs. Here, we establish the importance of Sal proteins as a common source of PLM resistance across multiple species of staphylococci. Sal(A) is revealed as but one member of a larger group of Sal-type ABC-F proteins that vary considerably in their ability to mediate resistance to PLMs and other antibiotics. We find that specific sal genes are intrinsic to particular staphylococcal species, and show that this gene family is likely ancestral to the genus Staphylococcus. Finally, we solve the cryo-EM structure of a representative Sal-type protein (Sal(B)) in complex with the staphylococcal 70S ribosome, revealing that Sal-type proteins bind into the E site to mediate target protection, likely by displacing PLMs and other antibiotics via an allosteric mechanism. #1: Journal: Nucleic Acids Res. / Year: 2022 Title: Sal-type ABC-F proteins: intrinsic and common mediators of pleuromutilin resistance by target protection in staphylococci Authors: Mohamad M / Nicholson D / Saha CK / Hauryliuk V / Edwards TA / Atkinson GC / Ranson NA / O'Neill AJ | |||||||||
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_13191.map.gz | 152.2 MB | EMDB map data format | |
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Header (meta data) | emd-13191-v30.xml emd-13191.xml | 69.9 KB 69.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_13191_fsc.xml | 14.7 KB | Display | FSC data file |
Images | emd_13191.png | 134.6 KB | ||
Masks | emd_13191_msk_1.map emd_13191_msk_2.map | 274.6 MB 274.6 MB | Mask map | |
Others | emd_13191_additional_1.map.gz emd_13191_additional_2.map.gz emd_13191_half_map_1.map.gz emd_13191_half_map_2.map.gz | 149 MB 149 MB 218.5 MB 218.5 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13191 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13191 | HTTPS FTP |
-Validation report
Summary document | emd_13191_validation.pdf.gz | 564.6 KB | Display | EMDB validaton report |
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Full document | emd_13191_full_validation.pdf.gz | 564.1 KB | Display | |
Data in XML | emd_13191_validation.xml.gz | 22.6 KB | Display | |
Data in CIF | emd_13191_validation.cif.gz | 29.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13191 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13191 | HTTPS FTP |
-Related structure data
Related structure data | 7p48MC 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_13191.map.gz / Format: CCP4 / Size: 274.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | consensus map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_13191_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Mask #2
File | emd_13191_msk_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: 30S body map (after multibody refinement)
File | emd_13191_additional_1.map | ||||||||||||
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Annotation | 30S body map (after multibody refinement) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: 30S head map (after multibody refinement)
File | emd_13191_additional_2.map | ||||||||||||
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Annotation | 30S head map (after multibody refinement) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 1
File | emd_13191_half_map_1.map | ||||||||||||
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Annotation | Half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 2
File | emd_13191_half_map_2.map | ||||||||||||
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Annotation | Half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Staphylococcus ribosome in complex with Sal(B)
+Supramolecule #1: Staphylococcus ribosome in complex with Sal(B)
+Macromolecule #1: 50S ribosomal protein L33
+Macromolecule #2: 50S ribosomal protein L34
+Macromolecule #3: 50S ribosomal protein L35
+Macromolecule #4: 50S ribosomal protein L36
+Macromolecule #6: ABC-F type ribosomal protection protein
+Macromolecule #10: 50S ribosomal protein L2
+Macromolecule #11: 50S ribosomal protein L3
+Macromolecule #12: 50S ribosomal protein L4
+Macromolecule #13: 50S ribosomal protein L5
+Macromolecule #14: 50S ribosomal protein L6
+Macromolecule #15: 50S ribosomal protein L13
+Macromolecule #16: 50S ribosomal protein L14
+Macromolecule #17: 50S ribosomal protein L15
+Macromolecule #18: 50S ribosomal protein L16
+Macromolecule #19: 50S ribosomal protein L17
+Macromolecule #20: 50S ribosomal protein L18
+Macromolecule #21: 50S ribosomal protein L19
+Macromolecule #22: 50S ribosomal protein L20
+Macromolecule #23: 50S ribosomal protein L21
+Macromolecule #24: 50S ribosomal protein L22
+Macromolecule #25: 50S ribosomal protein L23
+Macromolecule #26: 50S ribosomal protein L24
+Macromolecule #27: 50S ribosomal protein L25
+Macromolecule #28: LSU ribosomal protein L27P
+Macromolecule #29: 50S ribosomal protein L28
+Macromolecule #30: 50S ribosomal protein L29
+Macromolecule #31: 50S ribosomal protein L30
+Macromolecule #32: 50S ribosomal protein L31 type B
+Macromolecule #33: 50S ribosomal protein L32
+Macromolecule #35: 30S ribosomal protein S2
+Macromolecule #36: 30S ribosomal protein S3
+Macromolecule #37: 30S ribosomal protein S4
+Macromolecule #38: 30S ribosomal protein S5
+Macromolecule #39: 30S ribosomal protein S6
+Macromolecule #40: 30S ribosomal protein S7
+Macromolecule #41: 30S ribosomal protein S8
+Macromolecule #42: 30S ribosomal protein S9
+Macromolecule #43: 30S ribosomal protein S10
+Macromolecule #44: 30S ribosomal protein S11
+Macromolecule #45: 30S ribosomal protein S12
+Macromolecule #46: 30S ribosomal protein S13
+Macromolecule #47: 30S ribosomal protein S14 type Z
+Macromolecule #48: 30S ribosomal protein S15
+Macromolecule #49: 30S ribosomal protein S16
+Macromolecule #50: 30S ribosomal protein S17
+Macromolecule #51: 30S ribosomal protein S18
+Macromolecule #52: 30S ribosomal protein S19
+Macromolecule #53: 30S ribosomal protein S20
+Macromolecule #5: P-site tRNA
+Macromolecule #7: mRNA
+Macromolecule #8: 23S rRNA
+Macromolecule #9: 5S rRNA
+Macromolecule #34: 16S rRNA
+Macromolecule #54: ZINC ION
+Macromolecule #55: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #56: MAGNESIUM ION
-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: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 60.0 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 |