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- EMDB-27930: Escherichia coli Rho-dependent transcription pre-termination comp... -
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Open data
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Basic information
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Title | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, lambda-tR1 rut RNA, Mg-ADP-BeF3, and NusG; TEC part | |||||||||
![]() | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, lambda-tR1 rut RNA, Mg-ADP-BeF3, and NusG; TEC part | |||||||||
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Function / homology | ![]() transcription elongation-coupled chromatin remodeling / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / DNA-directed RNA polymerase complex / transcription elongation factor complex ...transcription elongation-coupled chromatin remodeling / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / DNA-directed RNA polymerase complex / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription initiation / cell motility / DNA-templated transcription termination / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / response to heat / intracellular iron ion homeostasis / protein dimerization activity / response to antibiotic / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.27 Å | |||||||||
![]() | Molodtsov V / Wang C | |||||||||
Funding support | ![]()
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![]() | ![]() 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: ![]() Title: Structural basis of Rho-dependent transcription termination Authors: Molodtsov V / Wang C / Firlar E / Kaelber JT / Ebright RH | |||||||||
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 153.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 25.2 KB 25.2 KB | Display Display | ![]() |
Images | ![]() | 28.6 KB | ||
Others | ![]() ![]() | 153.8 MB 154.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8e6xMC ![]() 8e3fC ![]() 8e3hC ![]() 8e5kC ![]() 8e5lC ![]() 8e5oC ![]() 8e5pC ![]() 8e6wC ![]() 8e6zC ![]() 8e70C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, lambda-tR1 rut RNA, Mg-ADP-BeF3, and NusG; TEC part | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.069 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half-map 1 Escherichia coli Rho-dependent transcription pre-termination complex...
File | emd_27930_half_map_1.map | ||||||||||||
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Annotation | Half-map 1 Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, lambda-tR1 rut RNA, Mg-ADP-BeF3, and NusG; TEC part | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-map 2 Escherichia coli Rho-dependent transcription pre-termination complex...
File | emd_27930_half_map_2.map | ||||||||||||
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Annotation | Half-map 2 Escherichia coli Rho-dependent transcription pre-termination complex containing 18 nt long RNA spacer, lambda-tR1 rut RNA, Mg-ADP-BeF3, and NusG; TEC part | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Escherichia coli Rho-dependent transcription pre-termination comp...
+Supramolecule #1: Escherichia coli Rho-dependent transcription pre-termination comp...
+Macromolecule #1: NT DNA
+Macromolecule #2: T DNA
+Macromolecule #3: RNA with 18 nt long spacer
+Macromolecule #4: DNA-directed RNA polymerase subunit beta
+Macromolecule #5: DNA-directed RNA polymerase subunit beta'
+Macromolecule #6: DNA-directed RNA polymerase subunit alpha
+Macromolecule #7: DNA-directed RNA polymerase subunit omega
+Macromolecule #8: Transcription termination/antitermination protein NusG
+Macromolecule #9: MAGNESIUM ION
+Macromolecule #10: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.9 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 52.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
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: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.27 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 69316 |
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Initial angle assignment | Type: COMMON LINE |
Final angle assignment | Type: COMMON LINE |