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Yorodumi- EMDB-3713: 2.9 A cryo-EM structure of VemP-stalled ribosome-nascent chain complex -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-3713 | |||||||||
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Title | 2.9 A cryo-EM structure of VemP-stalled ribosome-nascent chain complex | |||||||||
Map data | ||||||||||
Sample |
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Keywords | VemP-SRC / peptidyltransferase center / ribosomal exit tunnel / helix-loop-helix. ribosome / 70S / ribosome stalling / arrest peptide / ribosome | |||||||||
Function / homology | Function and homology information negative regulation of cytoplasmic translational initiation / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity ...negative regulation of cytoplasmic translational initiation / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / translational termination / DnaA-L2 complex / four-way junction DNA binding / translation repressor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / cytosolic ribosome assembly / transcription elongation factor complex / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / translational initiation / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / regulation of translation / ribosomal small subunit assembly / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Vibrio alginolyticus (bacteria) / Escherichia coli K-12 (bacteria) / Escherichia coli (strain K12) (bacteria) / Escherichia coli (E. coli) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Su T | |||||||||
Citation | Journal: Elife / Year: 2017 Title: The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling. Authors: Ting Su / Jingdong Cheng / Daniel Sohmen / Rickard Hedman / Otto Berninghausen / Gunnar von Heijne / Daniel N Wilson / Roland Beckmann / Abstract: Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ...Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environment for initial protein folding events. Here, we present a 2.9 Å cryo-electron microscopy structure of a ribosome stalled during translation of the extremely compacted VemP nascent chain. The nascent chain forms two α-helices connected by an α-turn and a loop, enabling a total of 37 amino acids to be observed within the first 50-55 Å of the exit tunnel. The structure reveals how α-helix formation directly within the peptidyltransferase center of the ribosome interferes with aminoacyl-tRNA accommodation, suggesting that during canonical translation, a major role of the exit tunnel is to prevent excessive secondary structure formation that can interfere with the peptidyltransferase activity of the ribosome. | |||||||||
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_3713.map.gz | 175.2 MB | EMDB map data format | |
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Header (meta data) | emd-3713-v30.xml emd-3713.xml | 77.3 KB 77.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_3713_fsc.xml | 10.4 KB | Display | FSC data file |
Images | emd_3713.png | 264.3 KB | ||
Filedesc metadata | emd-3713.cif.gz | 13.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-3713 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-3713 | HTTPS FTP |
-Validation report
Summary document | emd_3713_validation.pdf.gz | 639.1 KB | Display | EMDB validaton report |
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Full document | emd_3713_full_validation.pdf.gz | 638.6 KB | Display | |
Data in XML | emd_3713_validation.xml.gz | 12.2 KB | Display | |
Data in CIF | emd_3713_validation.cif.gz | 16.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-3713 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-3713 | HTTPS FTP |
-Related structure data
Related structure data | 5nwyMC 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_3713.map.gz / Format: CCP4 / Size: 190.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.084 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 : VemP-stalled ribosome-nascent chain complex
+Supramolecule #1: VemP-stalled ribosome-nascent chain complex
+Supramolecule #2: VemP-stalled ribosome-nascent chain complex
+Supramolecule #3: VemP-stalled ribosome-nascent chain complex
+Supramolecule #4: VemP-stalled ribosome-nascent chain complex
+Macromolecule #1: VemP nascent chain
+Macromolecule #4: 50S ribosomal protein L2
+Macromolecule #5: 50S ribosomal protein L3
+Macromolecule #6: 50S ribosomal protein L4
+Macromolecule #7: 50S ribosomal protein L5
+Macromolecule #8: 50S ribosomal protein L6
+Macromolecule #9: 50S ribosomal protein L9
+Macromolecule #10: 50S ribosomal protein L11
+Macromolecule #11: 50S ribosomal protein L13
+Macromolecule #12: 50S ribosomal protein L14
+Macromolecule #13: 50S ribosomal protein L15
+Macromolecule #14: 50S ribosomal protein L16
+Macromolecule #15: 50S ribosomal protein L17
+Macromolecule #16: 50S ribosomal protein L18
+Macromolecule #17: 50S ribosomal protein L19
+Macromolecule #18: 50S ribosomal protein L20
+Macromolecule #19: 50S ribosomal protein L21
+Macromolecule #20: 50S ribosomal protein L22
+Macromolecule #21: 50S ribosomal protein L23
+Macromolecule #22: 50S ribosomal protein L24
+Macromolecule #23: 50S ribosomal protein L25
+Macromolecule #24: 50S ribosomal protein L27
+Macromolecule #25: 50S ribosomal protein L28
+Macromolecule #26: 50S ribosomal protein L29
+Macromolecule #27: 50S ribosomal protein L30
+Macromolecule #28: 50S ribosomal protein L32
+Macromolecule #29: 50S ribosomal protein L33
+Macromolecule #30: 50S ribosomal protein L34
+Macromolecule #31: 50S ribosomal protein L35
+Macromolecule #32: 50S ribosomal protein L36
+Macromolecule #34: 50S ribosomal protein L31
+Macromolecule #36: 30S ribosomal protein S2
+Macromolecule #37: 30S ribosomal protein S3
+Macromolecule #38: 30S ribosomal protein S4
+Macromolecule #39: 30S ribosomal protein S5
+Macromolecule #40: 30S ribosomal protein S6
+Macromolecule #41: 30S ribosomal protein S7
+Macromolecule #42: 30S ribosomal protein S8
+Macromolecule #43: 30S ribosomal protein S9
+Macromolecule #44: 30S ribosomal protein S10
+Macromolecule #45: 30S ribosomal protein S11
+Macromolecule #46: 30S ribosomal protein S12
+Macromolecule #47: 30S ribosomal protein S13
+Macromolecule #48: 30S ribosomal protein S14
+Macromolecule #49: 30S ribosomal protein S15
+Macromolecule #50: 30S ribosomal protein S16
+Macromolecule #51: 30S ribosomal protein S17
+Macromolecule #52: 30S ribosomal protein S18
+Macromolecule #53: 30S ribosomal protein S19
+Macromolecule #54: 30S ribosomal protein S20
+Macromolecule #55: 30S ribosomal protein S21
+Macromolecule #2: Gln-tRNA
+Macromolecule #3: 5S rRNA
+Macromolecule #33: 23S rRNA
+Macromolecule #35: 16S rRNA
+Macromolecule #56: mRNA
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 2.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | PDB-5nwy: |