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Yorodumi- PDB-9w0n: Escherichia coli transcription-translation coupled complex class ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9w0n | |||||||||||||||||||||
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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 | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||||||||||||||
Authors | Zhang, J. / Wang, C. | |||||||||||||||||||||
| Funding support | China, 1items
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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
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9w0n.cif.gz | 4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9w0n.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9w0n.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w0/9w0n ftp://data.pdbj.org/pub/pdb/validation_reports/w0/9w0n | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 65509MC ![]() 8vkvC ![]() 8vl1C ![]() 8vooC ![]() 8vopC ![]() 8voqC ![]() 8vorC ![]() 8vosC ![]() 9y79C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 6 types, 6 molecules 123654
| #1: RNA chain | Mass: 941612.375 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: RNA chain | Mass: 38790.090 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #3: RNA chain | Mass: 499690.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #5: RNA chain | Mass: 24802.785 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #37: RNA chain | Mass: 24485.539 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #58: RNA chain | Mass: 17502.830 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
+Large ribosomal subunit protein ... , 30 types, 30 molecules bcdefgijklmnopqrstuvwxyzABCDEF
-Transcription termination/antitermination protein ... , 2 types, 2 molecules NA7
| #36: Protein | Mass: 54932.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #63: Protein | Mass: 20044.941 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Small ribosomal subunit protein ... , 20 types, 20 molecules GHIJKLMNOPQRSTUVWXYZ
| #38: Protein | Mass: 26781.670 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #39: Protein | Mass: 26031.316 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #40: Protein | Mass: 23514.199 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #41: Protein | Mass: 17629.398 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #42: Protein | Mass: 15727.512 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #43: Protein | Mass: 20055.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #44: Protein | Mass: 14146.557 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #45: Protein | Mass: 14886.270 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #46: Protein | Mass: 11755.597 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #47: Protein | Mass: 13870.975 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #48: Protein | Mass: 13768.157 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #49: Protein | Mass: 13128.467 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #50: Protein | Mass: 11606.560 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #51: Protein | Mass: 10290.816 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #52: Protein | Mass: 9207.572 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #53: Protein | Mass: 9724.491 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #54: Protein | Mass: 9005.472 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #55: Protein | Mass: 10455.355 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #56: Protein | Mass: 9708.464 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #57: Protein | Mass: 8524.039 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-DNA-directed RNA polymerase subunit ... , 4 types, 5 molecules B2ahAABA
| #59: Protein | Mass: 150820.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rpoB, groN, nitB, rif, ron, stl, stv, tabD, b3987, JW3950 Production host: ![]() | ||||
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| #62: Protein | Mass: 36155.223 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #64: Protein | | Mass: 9291.407 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #65: Protein | | Mass: 150436.344 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-DNA chain , 2 types, 2 molecules 98
| #60: DNA chain | Mass: 11473.346 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #61: DNA chain | Mass: 11230.182 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein / Non-polymers , 2 types, 2 molecules 0

| #4: Protein | Mass: 77676.227 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P0A6M8, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
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| #66: Chemical | ChemComp-MG / |
-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: NusA-NusG-TTC-Bwalked / Type: COMPLEX / Entity ID: #1-#35, #37-#58, #60-#61 / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.6 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1717500 / Symmetry type: POINT |
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FIELD EMISSION GUN