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- PDB-6vyu: Escherichia coli transcription-translation complex C2 (TTC-C2) co... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6vyu | ||||||
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Title | Escherichia coli transcription-translation complex C2 (TTC-C2) containing a 27 nt long mRNA spacer | ||||||
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![]() | RIBOSOME / TRANSCRIPTION/TRANSLATION / Bacterial transcription-translation coupled complex / TRANSCRIPTION / TRANSCRIPTION-TRANSLATION complex | ||||||
Function / homology | ![]() transcription elongation-coupled chromatin remodeling / DNA-directed RNA polymerase complex / DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / regulation of DNA-templated transcription elongation / ribosomal large subunit assembly / transcription antitermination / DNA-templated transcription termination / ribonucleoside binding / mRNA 5'-UTR binding ...transcription elongation-coupled chromatin remodeling / DNA-directed RNA polymerase complex / DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / regulation of DNA-templated transcription elongation / ribosomal large subunit assembly / transcription antitermination / DNA-templated transcription termination / ribonucleoside binding / mRNA 5'-UTR binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / large ribosomal subunit / small ribosomal subunit / small ribosomal subunit rRNA binding / transferase activity / 5S rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / protein dimerization activity / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / DNA-templated transcription / magnesium ion binding / DNA binding / RNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() synthetic construct (others) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7 Å | ||||||
![]() | Molodtsov, V. / Wang, C. / Su, M. / Ebright, R.H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of transcription-translation coupling. Authors: Chengyuan Wang / Vadim Molodtsov / Emre Firlar / Jason T Kaelber / Gregor Blaha / Min Su / Richard H Ebright / ![]() Abstract: In bacteria, transcription and translation are coupled processes in which the movement of RNA polymerase (RNAP)-synthesizing messenger RNA (mRNA) is coordinated with the movement of the first ...In bacteria, transcription and translation are coupled processes in which the movement of RNA polymerase (RNAP)-synthesizing messenger RNA (mRNA) is coordinated with the movement of the first ribosome-translating mRNA. Coupling is modulated by the transcription factors NusG (which is thought to bridge RNAP and the ribosome) and NusA. Here, we report cryo-electron microscopy structures of transcription-translation complexes (TTCs) containing different-length mRNA spacers between RNAP and the ribosome active-center P site. Structures of TTCs containing short spacers show a state incompatible with NusG bridging and NusA binding (TTC-A, previously termed "expressome"). Structures of TTCs containing longer spacers reveal a new state compatible with NusG bridging and NusA binding (TTC-B) and reveal how NusG bridges and NusA binds. We propose that TTC-B mediates NusG- and NusA-dependent transcription-translation coupling. | ||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 6.7 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 21472MC ![]() 6vu3C ![]() 6vyqC ![]() 6vyrC ![]() 6vysC ![]() 6vytC ![]() 6vywC ![]() 6vyxC ![]() 6vyyC ![]() 6vyzC ![]() 6vz2C ![]() 6vz3C ![]() 6vz5C ![]() 6vz7C ![]() 6vzjC ![]() 6x6tC ![]() 6x7fC ![]() 6x7kC ![]() 6x9qC ![]() 6xdqC ![]() 6xdrC ![]() 6xgfC ![]() 6xiiC ![]() 6xijC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
+50S ribosomal protein ... , 29 types, 29 molecules 01234bcefghijklmnopqrstuvwxyz
-DNA chain , 2 types, 2 molecules 56
#6: DNA chain | Mass: 11042.110 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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#7: DNA chain | Mass: 10956.012 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-RNA chain , 6 types, 7 molecules 7ABDYad
#8: RNA chain | Mass: 5196.096 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) | ||||||||
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#9: RNA chain | Mass: 24496.617 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #16: RNA chain | | Mass: 499690.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #37: RNA chain | | Mass: 873.540 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) #38: RNA chain | | Mass: 941635.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #41: RNA chain | | Mass: 38790.090 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 AAACADAEAF
#10: Protein | Mass: 150820.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#12: Protein | Mass: 36558.680 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: A0A073G207, DNA-directed RNA polymerase #13: Protein | | Mass: 155366.781 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: A0A4S1NBU2, DNA-directed RNA polymerase #14: Protein | | Mass: 10249.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: A0A070UPX4, DNA-directed RNA polymerase |
-Protein , 1 types, 1 molecules AB
#11: Protein | Mass: 20560.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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+30S ribosomal protein ... , 21 types, 21 molecules CEFGHIJKLMNOPQRSTUVWX
-Non-polymers , 2 types, 3 molecules ![](data/chem/img/MG.gif)
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#64: Chemical | ChemComp-MG / |
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#65: Chemical |
-Details
Has ligand of interest | N |
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-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: Escherichia coli transcription-translation complex C2 (TTC-C2) containing a 27 nt long mRNA spacer, NusG, and fMet-tRNAs in E-site and P-site Type: COMPLEX / Entity ID: #1-#63 / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8928 / Symmetry type: POINT |