+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-18534 | |||||||||
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Title | Structure of SecM-stalled Escherichia coli 70S ribosome | |||||||||
Map data | ||||||||||
Sample |
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Keywords | SecM / SRC / Stalling / Arrest Peptide / Arrest Motive / Stalling Motive / Stalled Ribosome Complex / SecA / Secretion Monitor / Leader Peptide / TRANSLATION / RIBOSOME | |||||||||
Function / homology | Function and homology information negative regulation of cytoplasmic translational initiation / 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 translational initiation / 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 / translation regulator activity / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / negative regulation of translational 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 / transcription elongation factor complex / cytosolic ribosome assembly / 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 / 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 / molecular adaptor activity / periplasmic space / 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 | Escherichia coli BW25113 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.0 Å | |||||||||
Authors | Gersteuer F / Morici M / Wilson DN | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nat Commun / Year: 2024 Title: The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome. Authors: Felix Gersteuer / Martino Morici / Sara Gabrielli / Keigo Fujiwara / Haaris A Safdari / Helge Paternoga / Lars V Bock / Shinobu Chiba / Daniel N Wilson / Abstract: Nascent polypeptide chains can induce translational stalling to regulate gene expression. This is exemplified by the E. coli secretion monitor (SecM) arrest peptide that induces translational ...Nascent polypeptide chains can induce translational stalling to regulate gene expression. This is exemplified by the E. coli secretion monitor (SecM) arrest peptide that induces translational stalling to regulate expression of the downstream encoded SecA, an ATPase that co-operates with the SecYEG translocon to facilitate insertion of proteins into or through the cytoplasmic membrane. Here we present the structure of a ribosome stalled during translation of the full-length E. coli SecM arrest peptide at 2.0 Å resolution. The structure reveals that SecM arrests translation by stabilizing the Pro-tRNA in the A-site, but in a manner that prevents peptide bond formation with the SecM-peptidyl-tRNA in the P-site. By employing molecular dynamic simulations, we also provide insight into how a pulling force on the SecM nascent chain can relieve the SecM-mediated translation arrest. Collectively, the mechanisms determined here for SecM arrest and relief are also likely to be applicable for a variety of other arrest peptides that regulate components of the protein localization machinery identified across a wide range of bacteria lineages. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_18534.map.gz | 193.1 MB | EMDB map data format | |
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Header (meta data) | emd-18534-v30.xml emd-18534.xml | 72.4 KB 72.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_18534_fsc.xml | 14.1 KB | Display | FSC data file |
Images | emd_18534.png | 177.8 KB | ||
Filedesc metadata | emd-18534.cif.gz | 14.3 KB | ||
Others | emd_18534_half_map_1.map.gz emd_18534_half_map_2.map.gz | 193.6 MB 193.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18534 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18534 | HTTPS FTP |
-Validation report
Summary document | emd_18534_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_18534_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_18534_validation.xml.gz | 21.2 KB | Display | |
Data in CIF | emd_18534_validation.cif.gz | 27.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18534 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18534 | HTTPS FTP |
-Related structure data
Related structure data | 8qoaMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_18534.map.gz / Format: CCP4 / Size: 244.1 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: 0.83 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_18534_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_18534_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : SecM-stalled ribosome complex
+Supramolecule #1: SecM-stalled ribosome complex
+Macromolecule #1: Large ribosomal subunit protein bL33
+Macromolecule #2: Large ribosomal subunit protein bL34
+Macromolecule #3: Large ribosomal subunit protein bL35
+Macromolecule #4: Large ribosomal subunit protein bL36A
+Macromolecule #6: 30S ribosomal protein S2
+Macromolecule #7: Small ribosomal subunit protein uS3
+Macromolecule #8: Small ribosomal subunit protein uS4
+Macromolecule #9: Small ribosomal subunit protein uS5
+Macromolecule #10: 30S ribosomal protein S6, fully modified isoform
+Macromolecule #11: 30S ribosomal protein S7
+Macromolecule #12: Small ribosomal subunit protein uS8
+Macromolecule #13: Small ribosomal subunit protein uS9
+Macromolecule #14: Small ribosomal subunit protein uS12
+Macromolecule #15: Small ribosomal subunit protein uS13
+Macromolecule #16: Small ribosomal subunit protein uS14
+Macromolecule #17: Small ribosomal subunit protein uS15
+Macromolecule #18: 30S ribosomal protein S16
+Macromolecule #19: Small ribosomal subunit protein uS17
+Macromolecule #20: Small ribosomal subunit protein bS18
+Macromolecule #21: Small ribosomal subunit protein uS19
+Macromolecule #22: 30S ribosomal protein S20
+Macromolecule #23: Small ribosomal subunit protein bS21
+Macromolecule #27: Large ribosomal subunit protein uL2
+Macromolecule #28: Large ribosomal subunit protein uL3
+Macromolecule #29: Large ribosomal subunit protein uL4
+Macromolecule #30: Large ribosomal subunit protein uL5
+Macromolecule #31: Large ribosomal subunit protein uL6
+Macromolecule #32: Large ribosomal subunit protein bL9
+Macromolecule #33: Large ribosomal subunit protein uL13
+Macromolecule #34: Large ribosomal subunit protein uL14
+Macromolecule #35: 50S ribosomal protein L15
+Macromolecule #36: Large ribosomal subunit protein bL17
+Macromolecule #37: Large ribosomal subunit protein uL18
+Macromolecule #38: Large ribosomal subunit protein bL19
+Macromolecule #39: Large ribosomal subunit protein bL20
+Macromolecule #40: Large ribosomal subunit protein bL21
+Macromolecule #41: Large ribosomal subunit protein uL22
+Macromolecule #42: Large ribosomal subunit protein uL23
+Macromolecule #43: Large ribosomal subunit protein uL24
+Macromolecule #44: 50S ribosomal protein L25
+Macromolecule #45: Large ribosomal subunit protein bL27
+Macromolecule #46: Large ribosomal subunit protein bL28
+Macromolecule #47: Large ribosomal subunit protein uL29
+Macromolecule #48: Large ribosomal subunit protein uL30
+Macromolecule #49: Large ribosomal subunit protein bL32
+Macromolecule #51: Large ribosomal subunit protein bL31A
+Macromolecule #54: Small ribosomal subunit protein uS10
+Macromolecule #55: Secretion monitor
+Macromolecule #56: Large ribosomal subunit protein uL16
+Macromolecule #57: Small ribosomal subunit protein uS11
+Macromolecule #5: E-site tRNA
+Macromolecule #24: mRNA
+Macromolecule #25: P-site tRNA-gly
+Macromolecule #26: 5S rRNA
+Macromolecule #50: A-site tRNA-pro
+Macromolecule #52: 23S rRNA
+Macromolecule #53: 16S rRNA
+Macromolecule #58: ZINC ION
+Macromolecule #59: POTASSIUM ION
+Macromolecule #60: MAGNESIUM ION
+Macromolecule #61: PROLINE
+Macromolecule #62: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 0.9 µm / Nominal defocus min: 0.3 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |