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Yorodumi- EMDB-22141: Cryo-EM structure of an Escherichia coli coupled transcription-tr... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-22141 | |||||||||
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Title | Cryo-EM structure of an Escherichia coli coupled transcription-translation complex B3 (TTC-B3) containing an mRNA with a 30 nt long spacer, transcription factors NusA and NusG, and fMet-tRNAs at P-site and E-site | |||||||||
Map data | Transcription-translation complex B3 (TTC-B3) containing an mRNA with a 30 nt long spacer, transcription factors NusA and NusG, and fMet-tRNAs at P-site and E-site | |||||||||
Sample |
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Function / homology | Function and homology information DNA-templated transcription elongation / positive regulation of ribosome biogenesis / DnaA-L2 complex / DNA-directed RNA polymerase complex / negative regulation of DNA-templated DNA replication initiation / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / transcription antitermination / regulation of cell growth ...DNA-templated transcription elongation / positive regulation of ribosome biogenesis / DnaA-L2 complex / DNA-directed RNA polymerase complex / negative regulation of DNA-templated DNA replication initiation / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / ribonucleoside binding / mRNA 5'-UTR binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / protein dimerization activity / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / DNA-binding transcription factor activity / mRNA binding / nucleotide binding / DNA-templated transcription / magnesium ion binding / DNA binding / RNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) / synthetic construct (others) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Molodtsov V / Ebright RH / Wang C / Su M | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Science / Year: 2020 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
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_22141.map.gz | 411.2 MB | EMDB map data format | |
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Header (meta data) | emd-22141-v30.xml emd-22141.xml | 88.3 KB 88.3 KB | Display Display | EMDB header |
Images | emd_22141.png | 66 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-22141 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-22141 | HTTPS FTP |
-Validation report
Summary document | emd_22141_validation.pdf.gz | 516.3 KB | Display | EMDB validaton report |
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Full document | emd_22141_full_validation.pdf.gz | 515.9 KB | Display | |
Data in XML | emd_22141_validation.xml.gz | 8 KB | Display | |
Data in CIF | emd_22141_validation.cif.gz | 9.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-22141 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-22141 | HTTPS FTP |
-Related structure data
Related structure data | 6xdqMC 6vu3C 6vyqC 6vyrC 6vysC 6vytC 6vyuC 6vywC 6vyxC 6vyyC 6vyzC 6vz2C 6vz3C 6vz5C 6vz7C 6vzjC 6x6tC 6x7fC 6x7kC 6x9qC 6xdrC 6xgfC 6xiiC 6xijC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_22141.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Transcription-translation complex B3 (TTC-B3) containing an mRNA with a 30 nt long spacer, transcription factors NusA and NusG, and fMet-tRNAs at P-site and E-site | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : Cryo-EM structure of an Escherichia coli coupled transcription-tr...
+Supramolecule #1: Cryo-EM structure of an Escherichia coli coupled transcription-tr...
+Macromolecule #1: 50S ribosomal protein L21
+Macromolecule #2: 50S ribosomal protein L22
+Macromolecule #3: 50S ribosomal protein L23
+Macromolecule #4: 50S ribosomal protein L24
+Macromolecule #5: 50S ribosomal protein L25
+Macromolecule #9: 50S ribosomal protein L10
+Macromolecule #11: DNA-directed RNA polymerase subunit beta
+Macromolecule #12: Transcription termination/antitermination protein NusG
+Macromolecule #13: DNA-directed RNA polymerase subunit alpha
+Macromolecule #14: DNA-directed RNA polymerase subunit beta'
+Macromolecule #15: DNA-directed RNA polymerase subunit omega
+Macromolecule #16: Transcription termination/antitermination protein NusA
+Macromolecule #17: 30S ribosomal protein S18
+Macromolecule #19: 30S ribosomal protein S20
+Macromolecule #20: 30S ribosomal protein S21
+Macromolecule #21: 30S ribosomal protein S2
+Macromolecule #22: 30S ribosomal protein S1
+Macromolecule #23: 30S ribosomal protein S3
+Macromolecule #24: 30S ribosomal protein S4
+Macromolecule #25: 30S ribosomal protein S5
+Macromolecule #26: 30S ribosomal protein S6
+Macromolecule #27: 30S ribosomal protein S7
+Macromolecule #28: 30S ribosomal protein S8
+Macromolecule #29: 30S ribosomal protein S9
+Macromolecule #30: 30S ribosomal protein S10
+Macromolecule #31: 30S ribosomal protein S11
+Macromolecule #32: 30S ribosomal protein S12
+Macromolecule #33: 30S ribosomal protein S14
+Macromolecule #34: 30S ribosomal protein S15
+Macromolecule #35: 30S ribosomal protein S16
+Macromolecule #36: 30S ribosomal protein S17
+Macromolecule #37: 30S ribosomal protein S19
+Macromolecule #38: 30S ribosomal protein S13
+Macromolecule #39: 50S ribosomal protein L11
+Macromolecule #40: 50S ribosomal protein L7/L12
+Macromolecule #42: 50S ribosomal protein L27
+Macromolecule #43: 50S ribosomal protein L28
+Macromolecule #45: 50S ribosomal protein L29
+Macromolecule #46: 50S ribosomal protein L30
+Macromolecule #47: 50S ribosomal protein L31
+Macromolecule #48: 50S ribosomal protein L2
+Macromolecule #49: 50S ribosomal protein L32
+Macromolecule #50: 50S ribosomal protein L3
+Macromolecule #51: 50S ribosomal protein L33
+Macromolecule #52: 50S ribosomal protein L4
+Macromolecule #53: 50S ribosomal protein L34
+Macromolecule #54: 50S ribosomal protein L5
+Macromolecule #55: 50S ribosomal protein L35
+Macromolecule #56: 50S ribosomal protein L6
+Macromolecule #57: 50S ribosomal protein L36
+Macromolecule #58: 50S ribosomal protein L9
+Macromolecule #59: 50S ribosomal protein L13
+Macromolecule #60: 50S ribosomal protein L14
+Macromolecule #61: 50S ribosomal protein L15
+Macromolecule #62: 50S ribosomal protein L16
+Macromolecule #63: 50S ribosomal protein L17
+Macromolecule #64: 50S ribosomal protein L18
+Macromolecule #65: 50S ribosomal protein L19
+Macromolecule #66: 50S ribosomal protein L20
+Macromolecule #6: NT DNA
+Macromolecule #7: T DNA
+Macromolecule #8: mRNA with 30 nt long spacer
+Macromolecule #10: E-site and P-site tRNA (fMet)
+Macromolecule #18: 16S rRNA
+Macromolecule #41: 23S rRNA
+Macromolecule #44: 5S rRNA
+Macromolecule #67: MAGNESIUM ION
+Macromolecule #68: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.6 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 19967 |
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Initial angle assignment | Type: COMMON LINE |
Final angle assignment | Type: COMMON LINE |