+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-28720 | |||||||||
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Title | 30S_delta_ksgA+KsgA complex | |||||||||
Map data | Consensus | |||||||||
Sample |
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Keywords | Ribosome / KsgA | |||||||||
Function / homology | Function and homology information 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase / 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / transcription antitermination / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding ...16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase / 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / transcription antitermination / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / response to antibiotic / mRNA binding / RNA binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Sun J / Kinman LF / Jahagirdar D / Ortega J / Davis JH | |||||||||
Funding support | Canada, 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2023 Title: KsgA facilitates ribosomal small subunit maturation by proofreading a key structural lesion. Authors: Jingyu Sun / Laurel F Kinman / Dushyant Jahagirdar / Joaquin Ortega / Joseph H Davis / Abstract: Ribosome assembly is orchestrated by many assembly factors, including ribosomal RNA methyltransferases, whose precise role is poorly understood. Here, we leverage the power of cryo-EM and machine ...Ribosome assembly is orchestrated by many assembly factors, including ribosomal RNA methyltransferases, whose precise role is poorly understood. Here, we leverage the power of cryo-EM and machine learning to discover that the E. coli methyltransferase KsgA performs a 'proofreading' function in the assembly of the small ribosomal subunit by recognizing and partially disassembling particles that have matured but are not competent for translation. We propose that this activity allows inactive particles an opportunity to reassemble into an active state, thereby increasing overall assembly fidelity. Detailed structural quantifications in our datasets additionally enabled the expansion of the Nomura assembly map to highlight rRNA helix and r-protein interdependencies, detailing how the binding and docking of these elements are tightly coupled. These results have wide-ranging implications for our understanding of the quality-control mechanisms governing ribosome biogenesis and showcase the power of heterogeneity analysis in cryo-EM to unveil functionally relevant information in biological systems. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_28720.map.gz | 14.9 MB | EMDB map data format | |
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Header (meta data) | emd-28720-v30.xml emd-28720.xml | 41.8 KB 41.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_28720_fsc.xml | 13.5 KB | Display | FSC data file |
Images | emd_28720.png | 72.6 KB | ||
Filedesc metadata | emd-28720.cif.gz | 8.9 KB | ||
Others | emd_28720_additional_1.map.gz emd_28720_additional_2.map.gz emd_28720_additional_3.map.gz emd_28720_additional_4.map.gz emd_28720_half_map_1.map.gz emd_28720_half_map_2.map.gz | 190 MB 192.5 MB 194 MB 195.8 MB 168.1 MB 168.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28720 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28720 | HTTPS FTP |
-Related structure data
Related structure data | 8eytMC 8eyqC M: atomic model generated by this map C: citing same article (ref.) |
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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_28720.map.gz / Format: CCP4 / Size: 212.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Consensus | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.855 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Multibody body 1
File | emd_28720_additional_1.map | ||||||||||||
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Annotation | Multibody body 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Multibody body 2
File | emd_28720_additional_2.map | ||||||||||||
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Annotation | Multibody body 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Multibody body 3
File | emd_28720_additional_3.map | ||||||||||||
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Annotation | Multibody body 3 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Multibody composite
File | emd_28720_additional_4.map | ||||||||||||
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Annotation | Multibody composite | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_28720_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_28720_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 30S_delta_KsgA+KsgA
+Supramolecule #1: 30S_delta_KsgA+KsgA
+Macromolecule #1: 16S rRNA
+Macromolecule #2: 30S ribosomal protein S2
+Macromolecule #3: 30S ribosomal protein S4
+Macromolecule #4: 30S ribosomal protein S5
+Macromolecule #5: 30S ribosomal protein S8
+Macromolecule #6: 30S ribosomal protein S12
+Macromolecule #7: 30S ribosomal protein S16
+Macromolecule #8: 30S ribosomal protein S17
+Macromolecule #9: 30S ribosomal protein S20
+Macromolecule #10: 30S ribosomal protein S3
+Macromolecule #11: 30S ribosomal protein S7
+Macromolecule #12: 30S ribosomal protein S9
+Macromolecule #13: 30S ribosomal protein S10
+Macromolecule #14: 30S ribosomal protein S13
+Macromolecule #15: 30S ribosomal protein S14
+Macromolecule #16: 30S ribosomal protein S19
+Macromolecule #17: 30S ribosomal protein S6
+Macromolecule #18: 30S ribosomal protein S11
+Macromolecule #19: 30S ribosomal protein S15
+Macromolecule #20: 30S ribosomal protein S18
+Macromolecule #21: Ribosomal RNA small subunit methyltransferase A
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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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 K3 BIOQUANTUM (6k x 4k) / Average electron dose: 72.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |