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Open data
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Basic information
| Entry | Database: PDB / ID: 6tqo | ||||||
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| Title | rrn anti-termination complex | ||||||
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Keywords | TRANSCRIPTION / rrn / anti-termination complex / RNAP / Nus factors / SuhB / S4 | ||||||
| Function / homology | Function and homology information: / glycerol-2-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 3-phosphatase activity / lithium ion binding / inositol-phosphate phosphatase / inositol monophosphate 1-phosphatase activity / inositol metabolic process / DNA-templated transcription elongation / rRNA primary transcript binding ...: / glycerol-2-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 3-phosphatase activity / lithium ion binding / inositol-phosphate phosphatase / inositol monophosphate 1-phosphatase activity / inositol metabolic process / DNA-templated transcription elongation / rRNA primary transcript binding / transcription elongation-coupled chromatin remodeling / RNA polymerase complex / submerged biofilm formation / phosphatidylinositol phosphate biosynthetic process / 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 / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / bacterial-type flagellum-dependent cell motility / nitrate assimilation / negative regulation of translational initiation / DNA-directed RNA polymerase complex / mRNA regulatory element binding translation repressor activity / regulation of DNA-templated transcription elongation / transcription elongation factor complex / transcription antitermination / cell motility / DNA-templated transcription initiation / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / ribosome biogenesis / response to heat / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / protein-containing complex assembly / cytosolic small ribosomal subunit / intracellular iron ion homeostasis / cytoplasmic translation / tRNA binding / protein dimerization activity / rRNA binding / structural constituent of ribosome / ribosome / translation / DNA-binding transcription factor activity / protein domain specific binding / response to antibiotic / nucleotide binding / DNA-templated transcription / magnesium ion binding / signal transduction / DNA binding / RNA binding / zinc ion binding / metal ion binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | ||||||
Authors | Huang, Y.H. / Wahl, M.C. / Loll, B. / Hilal, T. / Said, N. | ||||||
Citation | Journal: Mol Cell / Year: 2020Title: Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine Required for Ribosome Biosynthesis. Authors: Yong-Heng Huang / Tarek Hilal / Bernhard Loll / Jörg Bürger / Thorsten Mielke / Christoph Böttcher / Nelly Said / Markus C Wahl / ![]() Abstract: Bacterial ribosomal RNAs are synthesized by a dedicated, conserved transcription-elongation complex that transcribes at high rates, shields RNA polymerase from premature termination, and supports co- ...Bacterial ribosomal RNAs are synthesized by a dedicated, conserved transcription-elongation complex that transcribes at high rates, shields RNA polymerase from premature termination, and supports co-transcriptional RNA folding, modification, processing, and ribosomal subunit assembly by presently unknown mechanisms. We have determined cryo-electron microscopy structures of complete Escherichia coli ribosomal RNA transcription elongation complexes, comprising RNA polymerase; DNA; RNA bearing an N-utilization-site-like anti-termination element; Nus factors A, B, E, and G; inositol mono-phosphatase SuhB; and ribosomal protein S4. Our structures and structure-informed functional analyses show that fast transcription and anti-termination involve suppression of NusA-stabilized pausing, enhancement of NusG-mediated anti-backtracking, sequestration of the NusG C-terminal domain from termination factor ρ, and the ρ blockade. Strikingly, the factors form a composite RNA chaperone around the RNA polymerase RNA-exit tunnel, which supports co-transcriptional RNA folding and annealing of distal RNA regions. Our work reveals a polymerase/chaperone machine required for biosynthesis of functional ribosomes. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6tqo.cif.gz | 919.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6tqo.ent.gz | 734.1 KB | Display | PDB format |
| PDBx/mmJSON format | 6tqo.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6tqo_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 6tqo_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 6tqo_validation.xml.gz | 148.6 KB | Display | |
| Data in CIF | 6tqo_validation.cif.gz | 230.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tq/6tqo ftp://data.pdbj.org/pub/pdb/validation_reports/tq/6tqo | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 10548MC ![]() 6tqnC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 3 types, 3 molecules TSB
| #1: Protein | Mass: 29066.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Protein | Mass: 29537.502 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #4: Protein | Mass: 15838.161 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli / Gene: nusB, CCU01_023355 / Production host: ![]() |
-Transcription termination/antitermination protein ... , 2 types, 2 molecules AG
| #3: Protein | Mass: 55030.789 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #6: Protein | Mass: 20817.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-30S ribosomal protein ... , 2 types, 2 molecules EC
| #5: Protein | Mass: 12012.884 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #11: Protein | Mass: 23656.354 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 UVWXY
| #7: Protein | Mass: 36558.680 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #8: Protein | | Mass: 10249.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #9: Protein | | Mass: 150820.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P0A8V4, UniProt: P0A8V2*PLUS, DNA-directed RNA polymerase #10: Protein | | Mass: 156748.203 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: S1HM87, UniProt: P0A8T7*PLUS, DNA-directed RNA polymerase |
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-RNA chain , 1 types, 1 molecules R
| #12: RNA chain | Mass: 27435.295 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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-DNA chain , 2 types, 2 molecules LK
| #13: DNA chain | Mass: 10645.824 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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| #14: DNA chain | Mass: 10821.972 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
-Non-polymers , 2 types, 5 molecules 


| #15: Chemical | | #16: Chemical | |
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-Details
| Has ligand of interest | Y |
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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
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| Molecular weight | Value: 670 kDa/nm / Experimental value: NO | ||||||||||||||||||||||||
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| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 283 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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| Microscopy | Model: FEI POLARA 300 |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 31000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm / Cs: 2 mm / C2 aperture diameter: 50 µm |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement | |||||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 33821 / Symmetry type: POINT | |||||||||||||||||||||||||||
| Refine LS restraints |
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