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Yorodumi- EMDB-27897: Escherichia coli Rho-dependent transcription pre-termination comp... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-27897 | |||||||||
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Title | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG | |||||||||
Map data | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG | |||||||||
Sample |
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Biological species | Escherichia coli (E. coli) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 12.0 Å | |||||||||
Authors | Molodtsov V / Wang C / Ebright RH | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Nature / Year: 2023 Title: Structural basis of Rho-dependent transcription termination. Authors: Vadim Molodtsov / Chengyuan Wang / Emre Firlar / Jason T Kaelber / Richard H Ebright / Abstract: Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription- ...Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription-translation-coupling quality control in Escherichia coli. Here we report the preparation of complexes that are functional in factor-dependent transcription termination from Rho, NusG, RNA polymerase (RNAP), and synthetic nucleic acid scaffolds, and we report cryogenic electron microscopy structures of the complexes. The structures show that functional factor-dependent pre-termination complexes contain a closed-ring Rho hexamer; have RNA threaded through the central channel of Rho; have 60 nucleotides of RNA interacting sequence-specifically with the exterior of Rho and 6 nucleotides of RNA interacting sequence-specifically with the central channel of Rho; have Rho oriented relative to RNAP such that ATP-dependent translocation by Rho exerts mechanical force on RNAP; and have NusG bridging Rho and RNAP. The results explain five decades of research on Rho and provide a foundation for understanding Rho's function. #1: Journal: Biorxiv / Year: 2022 Title: Structural basis of Rho-dependent transcription termination Authors: Molodtsov V / Wang C / Firlar E / Kaelber JT / Ebright RH | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_27897.map.gz | 7.7 MB | EMDB map data format | |
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Header (meta data) | emd-27897-v30.xml emd-27897.xml | 13 KB 13 KB | Display Display | EMDB header |
Images | emd_27897.png | 30.4 KB | ||
Others | emd_27897_half_map_1.map.gz emd_27897_half_map_2.map.gz | 171.1 MB 170.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-27897 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-27897 | HTTPS FTP |
-Validation report
Summary document | emd_27897_validation.pdf.gz | 740.6 KB | Display | EMDB validaton report |
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Full document | emd_27897_full_validation.pdf.gz | 740.1 KB | Display | |
Data in XML | emd_27897_validation.xml.gz | 15.2 KB | Display | |
Data in CIF | emd_27897_validation.cif.gz | 17.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-27897 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-27897 | HTTPS FTP |
-Related structure data
Related structure data | 8e3fC 8e3hC 8e5kC 8e5lC 8e5oC 8e5pC 8e6wC 8e6xC 8e6zC 8e70C C: citing same article (ref.) |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_27897.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.038 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Escherichia coli Rho-dependent transcription pre-termination complex containing 18...
File | emd_27897_half_map_1.map | ||||||||||||
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Annotation | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Escherichia coli Rho-dependent transcription pre-termination complex containing 18...
File | emd_27897_half_map_2.map | ||||||||||||
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Annotation | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Escherichia coli Rho-dependent transcription pre-termination comp...
Entire | Name: Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG |
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Components |
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-Supramolecule #1: Escherichia coli Rho-dependent transcription pre-termination comp...
Supramolecule | Name: Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, Mg-ADP-BeF3, and NusG type: complex / ID: 1 / Chimera: Yes / Parent: 0 |
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Source (natural) | Organism: Escherichia coli (E. coli) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.9 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 28.0 e/Å2 |
Electron beam | Acceleration voltage: 200 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: 1.25 µm |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 12.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 15936 |
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Initial angle assignment | Type: COMMON LINE |
Final angle assignment | Type: COMMON LINE |