+Open data
-Basic information
Entry | Database: PDB / ID: 6tqo | ||||||
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Title | rrn anti-termination complex | ||||||
Components |
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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 / lithium ion binding / inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / DNA-templated transcription elongation / inositol metabolic process / rRNA primary transcript binding ...: / glycerol-2-phosphatase activity / lithium ion binding / inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / DNA-templated transcription elongation / inositol metabolic process / rRNA primary transcript binding / transcription elongation-coupled chromatin remodeling / RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / protein complex oligomerization / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / phosphatidylinositol phosphate biosynthetic process / transcription antitermination factor activity, RNA binding / bacterial-type flagellum-dependent cell motility / nitrate assimilation / DNA-directed RNA polymerase complex / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / transcription elongation factor complex / regulation of DNA-templated transcription elongation / DNA-templated transcription initiation / transcription antitermination / cell motility / DNA-templated transcription termination / maintenance of translational fidelity / ribonucleoside binding / mRNA 5'-UTR binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / ribosomal small subunit biogenesis / ribosome biogenesis / ribosomal small subunit assembly / small ribosomal subunit / response to heat / cytosolic small ribosomal subunit / protein-containing complex assembly / cytoplasmic translation / intracellular iron ion homeostasis / tRNA binding / protein dimerization activity / rRNA binding / ribosome / structural constituent of 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 / membrane / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
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: 2020 Title: 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. | ||||||
History |
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-Structure visualization
Movie |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6tqo.cif.gz | 919.6 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 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 | 148.3 KB | Display | |
Data in CIF | 6tqo_validation.cif.gz | 229 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 (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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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.) Escherichia coli (E. coli) / Gene: B9S25_006930 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A5B7PBT3, UniProt: P0ADG4*PLUS |
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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.) Escherichia coli (E. coli) / Gene: suhB, ssyA, b2533, JW2517 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0ADG4, inositol-phosphate phosphatase |
#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: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A4P8C5Y7, UniProt: P0A780*PLUS |
-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.) Escherichia coli (E. coli) / Gene: nusA, CCU01_003250 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A4P8BVH6, UniProt: P0AFF6*PLUS |
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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.) Escherichia coli (E. coli) / Gene: nusG, HMPREF1611_01657 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: V0ZS55, UniProt: P0AFG0*PLUS |
-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.) Escherichia coli (E. coli) / Gene: rpsJ, AD31_3986 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A073G203, UniProt: P0A7R5*PLUS |
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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.) Escherichia coli (E. coli) / Gene: rpsD, EC23916_1156 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: I2X692, UniProt: P0A7V8*PLUS |
-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.) Escherichia coli (E. coli) / Gene: rpoA, pez, phs, sez, b3295, JW3257 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A7Z4, DNA-directed RNA polymerase #8: Protein | | Mass: 10249.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoZ, b3649, JW3624 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A800, DNA-directed RNA polymerase #9: Protein | | Mass: 150820.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoB, Z5560, ECs4910 / Production host: Escherichia coli BL21(DE3) (bacteria) 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.) Escherichia coli (E. coli) / Gene: rpoC, A1WS_04718 / Production host: Escherichia coli BL21(DE3) (bacteria) 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.) Escherichia coli (E. coli) |
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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.) Escherichia coli (E. coli) |
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#14: DNA chain | Mass: 10821.972 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Escherichia coli (E. coli) |
-Non-polymers , 2 types, 5 molecules
#15: Chemical | #16: Chemical | |
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-Details
Has ligand of interest | Y |
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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 |
-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 |
-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) |
-Processing
Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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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 | ||||||||||||||||||||||||
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