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Yorodumi- PDB-9y79: Escherichia coli transcription-translation loosely coupled comple... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9y79 | |||||||||||||||
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| Title | Escherichia coli transcription-translation loosely coupled complex (TTC-LC^walked) containing mRNA with a 39 nt long spacer, NusG, NusA, and fMet-tRNAs in E-site and P-site | |||||||||||||||
Components |
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Keywords | TRANSCRIPTION / TRANSLATION / RIBOSOME/TRANSFERASE/DNA/RNA / Transcription-translation coupled complex / RIBOSOME-TRANSFERASE-DNA-RNA complex | |||||||||||||||
| Function / homology | Function and homology informationstringent response / RNA polymerase complex / DNA-templated transcription elongation / 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 ...stringent response / RNA polymerase complex / DNA-templated transcription elongation / 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 / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / DnaA-L2 complex / 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 / transcription elongation factor complex / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / DNA-directed RNA polymerase complex / cell motility / transcription antitermination / 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 / large ribosomal subunit / response to heat / transferase activity / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / protein-containing complex assembly / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / 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 / negative regulation of DNA-templated transcription / nucleotide binding / mRNA binding / magnesium ion binding / DNA-templated transcription / DNA binding / RNA binding / zinc ion binding / membrane / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||
| Biological species | ![]() synthetic construct (others) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||||||||
Authors | Shandilya, S. / Wang, C. / Molodtsov, V. / Ebright, R.H. | |||||||||||||||
| Funding support | United States, 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 | 9y79.cif.gz | 6.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9y79.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9y79.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y7/9y79 ftp://data.pdbj.org/pub/pdb/validation_reports/y7/9y79 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72646MC ![]() 8vkvC ![]() 8vl1C ![]() 8vooC ![]() 8vopC ![]() 8voqC ![]() 8vorC ![]() 8vosC C: citing same article ( M: map data used to model this data |
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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
+Protein , 1 types, 1 molecules 0
+50S ribosomal protein ... , 18 types, 18 molecules 1239Ybcfghijkmoqvz
+Large ribosomal subunit protein ... , 13 types, 13 molecules 4Zelnprstuwxy
+DNA chain , 2 types, 2 molecules 56
+RNA chain , 5 types, 6 molecules 7ABDad
+DNA-directed RNA polymerase subunit ... , 4 types, 5 molecules AAACADAEAF
+Transcription termination/antitermination protein ... , 2 types, 2 molecules AGNG
+Small ribosomal subunit protein ... , 17 types, 17 molecules CEFHJKLMNOPSTUVWX
+30S ribosomal protein ... , 4 types, 4 molecules GIQR
+Non-polymers , 2 types, 3 molecules 


+Details
-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: Transcription-Translation coupled complex / Type: COMPLEX Entity ID: #7, #1-#5, #9-#10, #16-#27, #29-#66, #6, #8, #11, #28, #12-#15 Source: MULTIPLE SOURCES |
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| Molecular weight | Value: 2.8 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1 |
| 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 magnification: 130000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| Particle selection | Num. of particles selected: 592698 | ||||||||||||||||
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 31000 / Symmetry type: POINT | ||||||||||||||||
| Atomic model building | PDB-ID: 8VOQ Accession code: 8VOQ / Source name: PDB / Type: experimental model |
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About Yorodumi





United States, 1items
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