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Yorodumi- EMDB-65509: Escherichia coli transcription-translation coupled complex class ... -
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Basic information
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| Title | Escherichia coli transcription-translation coupled complex class B (TTC-B) that ribosome walking for 4 codons to a 9 codon mRNA spacer, and fMet-tRNAs in E-site and P-site of the ribosome | |||||||||
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Keywords | ribosome / RNA polymerase / translation / transcription / coupling / transcription-translation coupling / expressome/RIBOSOME | |||||||||
| Function / homology | Function and homology informationribosome disassembly / guanosine tetraphosphate binding / stringent response / RNA polymerase complex / negative regulation of cytoplasmic translational initiation / DNA-templated transcription elongation / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / protein complex oligomerization ...ribosome disassembly / guanosine tetraphosphate binding / stringent response / RNA polymerase complex / negative regulation of cytoplasmic translational initiation / DNA-templated transcription elongation / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / protein complex oligomerization / bacterial-type flagellum assembly / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / translational elongation / misfolded RNA binding / Group I intron splicing / transcription elongation factor complex / RNA folding / translation elongation factor activity / bacterial-type flagellum-dependent cell motility / nitrate assimilation / transcriptional attenuation / translational termination / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / four-way junction DNA binding / negative regulation of cytoplasmic translation / regulation of mRNA stability / translation repressor activity / 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 / response to reactive oxygen species / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / cell motility / transcription antitermination / DNA-directed RNA polymerase complex / DNA endonuclease activity / regulation of cell growth / DNA-templated transcription initiation / translational initiation / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / regulation of translation / large ribosomal subunit / response to heat / transferase activity / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / ribosome biogenesis / protein-containing complex assembly / 5S rRNA binding / 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 / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cytoplasmic translation / tRNA binding / protein dimerization activity / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / DNA-binding transcription factor activity / protein domain specific binding / response to antibiotic / negative regulation of DNA-templated transcription / hydrolase activity / nucleotide binding / mRNA binding / GTPase activity / GTP binding / magnesium ion binding / DNA-templated transcription / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Zhang J / Wang C | |||||||||
| Funding support | China, 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_65509.map.gz | 699.4 MB | EMDB map data format | |
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| Header (meta data) | emd-65509-v30.xml emd-65509.xml | 95.2 KB 95.2 KB | Display Display | EMDB header |
| Images | emd_65509.png | 65.2 KB | ||
| Filedesc metadata | emd-65509.cif.gz | 18.1 KB | ||
| Others | emd_65509_half_map_1.map.gz emd_65509_half_map_2.map.gz | 699.8 MB 700.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65509 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65509 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9w0nMC ![]() 8vkvC ![]() 8vl1C ![]() 8vooC ![]() 8vopC ![]() 8voqC ![]() 8vorC ![]() 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_65509.map.gz / Format: CCP4 / Size: 865.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.824 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_65509_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_65509_half_map_2.map | ||||||||||||
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Sample components
+Entire : NusA-NusG-TTC-Bwalked
+Supramolecule #1: NusA-NusG-TTC-Bwalked
+Macromolecule #1: 23S rRNA
+Macromolecule #2: 5S rRNA
+Macromolecule #3: 16S rRNA
+Macromolecule #5: tRNA(fMet)
+Macromolecule #37: tRNA(Phe)
+Macromolecule #58: mRNA
+Macromolecule #4: Elongation factor G
+Macromolecule #6: Large ribosomal subunit protein uL2
+Macromolecule #7: Large ribosomal subunit protein uL3
+Macromolecule #8: Large ribosomal subunit protein uL4
+Macromolecule #9: Large ribosomal subunit protein uL5
+Macromolecule #10: Large ribosomal subunit protein uL6
+Macromolecule #11: Large ribosomal subunit protein bL9
+Macromolecule #12: Large ribosomal subunit protein uL11
+Macromolecule #13: Large ribosomal subunit protein uL13
+Macromolecule #14: Large ribosomal subunit protein uL14
+Macromolecule #15: Large ribosomal subunit protein uL15
+Macromolecule #16: Large ribosomal subunit protein uL16
+Macromolecule #17: Large ribosomal subunit protein bL17
+Macromolecule #18: Large ribosomal subunit protein uL18
+Macromolecule #19: Large ribosomal subunit protein bL19
+Macromolecule #20: Large ribosomal subunit protein bL20
+Macromolecule #21: Large ribosomal subunit protein bL21
+Macromolecule #22: Large ribosomal subunit protein uL22
+Macromolecule #23: Large ribosomal subunit protein uL23
+Macromolecule #24: Large ribosomal subunit protein uL24
+Macromolecule #25: Large ribosomal subunit protein bL25
+Macromolecule #26: Large ribosomal subunit protein bL27
+Macromolecule #27: Large ribosomal subunit protein bL28
+Macromolecule #28: Large ribosomal subunit protein uL29
+Macromolecule #29: Large ribosomal subunit protein uL30
+Macromolecule #30: Large ribosomal subunit protein bL31
+Macromolecule #31: Large ribosomal subunit protein bL32
+Macromolecule #32: Large ribosomal subunit protein bL33
+Macromolecule #33: Large ribosomal subunit protein bL34
+Macromolecule #34: Large ribosomal subunit protein bL35
+Macromolecule #35: Large ribosomal subunit protein bL36A
+Macromolecule #36: Transcription termination/antitermination protein NusA
+Macromolecule #38: Small ribosomal subunit protein uS2
+Macromolecule #39: Small ribosomal subunit protein uS3
+Macromolecule #40: Small ribosomal subunit protein uS4
+Macromolecule #41: Small ribosomal subunit protein uS5
+Macromolecule #42: Small ribosomal subunit protein bS6, fully modified isoform
+Macromolecule #43: Small ribosomal subunit protein uS7
+Macromolecule #44: Small ribosomal subunit protein uS8
+Macromolecule #45: Small ribosomal subunit protein uS9
+Macromolecule #46: Small ribosomal subunit protein uS10
+Macromolecule #47: Small ribosomal subunit protein uS11
+Macromolecule #48: Small ribosomal subunit protein uS12
+Macromolecule #49: Small ribosomal subunit protein uS13
+Macromolecule #50: Small ribosomal subunit protein uS14
+Macromolecule #51: Small ribosomal subunit protein uS15
+Macromolecule #52: Small ribosomal subunit protein bS16
+Macromolecule #53: Small ribosomal subunit protein uS17
+Macromolecule #54: Small ribosomal subunit protein bS18
+Macromolecule #55: Small ribosomal subunit protein uS19
+Macromolecule #56: Small ribosomal subunit protein bS20
+Macromolecule #57: Small ribosomal subunit protein bS21
+Macromolecule #59: DNA-directed RNA polymerase subunit beta
+Macromolecule #62: DNA-directed RNA polymerase subunit alpha
+Macromolecule #63: Transcription termination/antitermination protein NusG
+Macromolecule #64: DNA-directed RNA polymerase subunit omega
+Macromolecule #65: DNA-directed RNA polymerase subunit beta'
+Macromolecule #60: non-templete DNA strand
+Macromolecule #61: templete DNA strand
+Macromolecule #66: MAGNESIUM 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: 7.6 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 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: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Authors
China, 1 items
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Processing
FIELD EMISSION GUN
