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Yorodumi- EMDB-43390: Escherichia coli transcription-translation loosely coupled comple... -
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Basic information
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| Title | Escherichia coli transcription-translation loosely coupled complex (TTC-LC) containing mRNA with a 51 nt long spacer, NusG, NusA, and fMet-tRNAs in E-site and P-site | |||||||||
Map data | Escherichia coli transcription-translation loosely coupled complex (TTC-LC) containing mRNA with a 51 nt long spacer, NusG, NusA, and fMet-tRNAs in E-site and P-site | |||||||||
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Keywords | Transcription / translation / coupling / NusG / NusA / ops / TTC | |||||||||
| Function / homology | Function and homology informationtranscription elongation-coupled chromatin remodeling / RNA polymerase complex / stringent response / negative regulation of cytoplasmic translational initiation / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex ...transcription elongation-coupled chromatin remodeling / RNA polymerase complex / stringent response / negative regulation of cytoplasmic translational initiation / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / misfolded RNA binding / Group I intron splicing / RNA folding / bacterial-type flagellum-dependent cell motility / nitrate assimilation / translational termination / positive regulation of ribosome biogenesis / DnaA-L2 complex / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / regulation of DNA-templated transcription elongation / transcription elongation factor complex / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / DNA-directed RNA polymerase complex / transcription antitermination / cell motility / DNA-templated transcription initiation / translational initiation / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / ribonucleoside binding / mRNA 5'-UTR binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / response to heat / ribosome binding / ribosomal small subunit biogenesis / 5S rRNA binding / protein-containing complex assembly / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / intracellular iron ion homeostasis / cytoplasmic translation / tRNA binding / protein dimerization activity / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / DNA-binding transcription factor activity / ribonucleoprotein complex / response to antibiotic / nucleotide binding / mRNA binding / DNA-templated transcription / magnesium ion binding / DNA binding / RNA binding / zinc ion binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Molodtsov V / Wang C / Ebright RH | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2026Title: Structural basis of long-range transcription-translation coupling. Authors: Chengyuan Wang / Vadim Molodtsov / Shashank Shandilya / Linlin You / Jing Zhang / Konstantin Kuznedelov / Bryce E Nickels / Jason T Kaelber / Gregor Blaha / Richard H Ebright / ![]() Abstract: Structures recently have been reported of molecular assemblies that mediate transcription-translation coupling in . In these molecular assemblies, termed "coupled transcription-translation complexes" ...Structures recently have been reported of molecular assemblies that mediate transcription-translation coupling in . In these molecular assemblies, termed "coupled transcription-translation complexes" or "TTC-B," RNA polymerase (RNAP) directly interacts with the ribosome, the transcription elongation factor NusG or its paralog RfaH forms a bridge between RNAP and ribosome, and the transcription elongation factor NusA optionally forms a second bridge between RNAP and ribosome. Here, we report structures of coupled transcription-translation complexes having mRNA spacers between RNAP and ribosome longer than the maximum-length mRNA spacer compatible with formation of TTC-B. The results define a class of coupled transcription-translation complex, termed "TTC-LC," where "LC" denotes "long-range coupling." TTC-LC differs from TTC-B by a ~60° rotation and ~70 Å translation of RNAP relative to ribosome, resulting in loss of direct interactions between RNAP and ribosome and creation of a ~70 Å gap between RNAP and ribosome. TTC-LC accommodates long mRNA spacers by looping out mRNA from the gap between RNAP and ribosome. We present evidence that TTC-LC is a functional intermediate in assembling and disassembling TTC-B, mediating pre-TTC-B transcription-translation coupling before a ribosome catches up to RNAP, and mediating post-TTC-B transcription-translation coupling after a ribosome stops moving and RNAP continues moving. We show that TTC-B, but not TTC-LC, is severely defective in RNA-hairpin-dependent transcription termination, and that both TTC-B and TTC-LC are severely defective in Rho-dependent transcription termination. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_43390.map.gz | 408.4 MB | EMDB map data format | |
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| Header (meta data) | emd-43390-v30.xml emd-43390.xml | 99.7 KB 99.7 KB | Display Display | EMDB header |
| Images | emd_43390.png | 78.7 KB | ||
| Filedesc metadata | emd-43390.cif.gz | 20.7 KB | ||
| Others | emd_43390_half_map_1.map.gz emd_43390_half_map_2.map.gz | 412.2 MB 412.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-43390 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-43390 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8vorMC ![]() 8vkvC ![]() 8vl1C ![]() 8vooC ![]() 8vopC ![]() 8voqC ![]() 8vosC ![]() 9y79C 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_43390.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Escherichia coli transcription-translation loosely coupled complex (TTC-LC) containing mRNA with a 51 nt long spacer, NusG, NusA, and fMet-tRNAs in E-site and P-site | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: unmasked half map 1
| File | emd_43390_half_map_1.map | ||||||||||||
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| Annotation | unmasked half map 1 | ||||||||||||
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| Density Histograms |
-Half map: unmasked half map 2
| File | emd_43390_half_map_2.map | ||||||||||||
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| Annotation | unmasked half map 2 | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Escherichia coli transcription-translation loosely coupled comple...
+Supramolecule #1: Escherichia coli transcription-translation loosely coupled comple...
+Macromolecule #1: Ribosomal protein L21
+Macromolecule #2: 50S ribosomal protein L22
+Macromolecule #3: 50S ribosomal protein L23
+Macromolecule #4: 50S ribosomal protein L24
+Macromolecule #5: 50S ribosomal protein L25
+Macromolecule #9: 50S ribosomal protein L10
+Macromolecule #11: DNA-directed RNA polymerase subunit beta
+Macromolecule #12: Transcription termination/antitermination protein NusG
+Macromolecule #13: DNA-directed RNA polymerase subunit alpha
+Macromolecule #14: DNA-directed RNA polymerase subunit beta'
+Macromolecule #15: DNA-directed RNA polymerase subunit omega
+Macromolecule #16: Transcription termination/antitermination protein NusA
+Macromolecule #17: 30S ribosomal protein S18
+Macromolecule #19: 30S ribosomal protein S20
+Macromolecule #20: 30S ribosomal protein S21
+Macromolecule #21: 30S ribosomal protein S2
+Macromolecule #22: 30S ribosomal protein S1
+Macromolecule #23: 30S ribosomal protein S3
+Macromolecule #24: 30S ribosomal protein S4
+Macromolecule #25: 30S ribosomal protein S5
+Macromolecule #26: 30S ribosomal protein S6
+Macromolecule #27: 30S ribosomal protein S7
+Macromolecule #28: 30S ribosomal protein S8
+Macromolecule #29: 30S ribosomal protein S9
+Macromolecule #30: 30S ribosomal protein S10
+Macromolecule #31: 30S ribosomal protein S11
+Macromolecule #32: 30S ribosomal protein S12
+Macromolecule #33: 30S ribosomal protein S14
+Macromolecule #34: Small ribosomal subunit protein uS15
+Macromolecule #35: 30S ribosomal protein S16
+Macromolecule #36: 30S ribosomal protein S17
+Macromolecule #37: 30S ribosomal protein S19
+Macromolecule #38: 30S ribosomal protein S13
+Macromolecule #39: 50S ribosomal protein L11
+Macromolecule #40: 50S ribosomal protein L7/L12
+Macromolecule #42: 50S ribosomal protein L27
+Macromolecule #43: 50S ribosomal protein L28
+Macromolecule #45: 50S ribosomal protein L29
+Macromolecule #46: 50S ribosomal protein L30
+Macromolecule #47: 50S ribosomal protein L31
+Macromolecule #48: 50S ribosomal protein L2
+Macromolecule #49: 50S ribosomal protein L32
+Macromolecule #50: 50S ribosomal protein L3
+Macromolecule #51: 50S ribosomal protein L33
+Macromolecule #52: 50S ribosomal protein L4
+Macromolecule #53: 50S ribosomal protein L34
+Macromolecule #54: 50S ribosomal protein L5
+Macromolecule #55: 50S ribosomal protein L35
+Macromolecule #56: 50S ribosomal protein L6
+Macromolecule #57: 50S ribosomal protein L36
+Macromolecule #58: 50S ribosomal protein L9
+Macromolecule #59: 50S ribosomal protein L13
+Macromolecule #60: 50S ribosomal protein L14
+Macromolecule #61: 50S ribosomal protein L15
+Macromolecule #62: 50S ribosomal protein L16
+Macromolecule #63: 50S ribosomal protein L17
+Macromolecule #64: 50S ribosomal protein L18
+Macromolecule #65: 50S ribosomal protein L19
+Macromolecule #66: 50S ribosomal protein L20
+Macromolecule #6: NT DNA
+Macromolecule #7: T DNA
+Macromolecule #8: mRNA with 51 nt long spacer
+Macromolecule #10: E-site and P-site tRNA (fMet)
+Macromolecule #18: 16S rRNA
+Macromolecule #41: 23S rRNA
+Macromolecule #44: 5S rRNA
+Macromolecule #67: MAGNESIUM ION
+Macromolecule #68: ZINC ION
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 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 |
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Keywords
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United States, 1 items
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Processing
FIELD EMISSION GUN
