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- EMDB-7341: Conformation of methylated GGQ in the peptidyl transferase center... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-7341 | |||||||||
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Title | Conformation of methylated GGQ in the peptidyl transferase center during translation termination | |||||||||
![]() | non-stop termination complex | |||||||||
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![]() | nonstop / termination / ArfA / RF2 / methylation / RIBOSOME | |||||||||
Function / homology | ![]() translation release factor activity, codon specific / negative regulation of cytoplasmic translational initiation / stringent response / ribosomal large subunit binding / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation ...translation release factor activity, codon specific / negative regulation of cytoplasmic translational initiation / stringent response / ribosomal large subunit binding / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / positive regulation of ribosome biogenesis / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / four-way junction DNA binding / translation repressor activity / rescue of stalled ribosome / negative regulation of translational initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / ribosome assembly / 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 / regulation of translation / ribosome biogenesis / large ribosomal subunit / ribosome binding / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / viral translational frameshifting / 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 | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.24 Å | |||||||||
![]() | Zeng F / Jin H | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination. Authors: Fuxing Zeng / Hong Jin / ![]() Abstract: The universally conserved Gly-Gly-Gln (GGQ) tripeptide in release factors or release factor-like surveillance proteins is required to catalyze the release of nascent peptide in the ribosome. The ...The universally conserved Gly-Gly-Gln (GGQ) tripeptide in release factors or release factor-like surveillance proteins is required to catalyze the release of nascent peptide in the ribosome. The glutamine of the GGQ is methylated post-translationally at the N position in vivo; this covalent modification is essential for optimal cell growth and efficient translation termination. However, the precise conformation of the methylated-GGQ tripeptide in the ribosome remains unknown. Using cryoEM and X-ray crystallography, we report the conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control. It has been suggested that the GGQ motif arose independently through convergent evolution among otherwise unrelated proteins that catalyze peptide release. The requirement for this tripeptide in the highly conserved peptidyl transferase center suggests that the conformation reported here is likely shared during termination of protein synthesis in all domains of life. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 202.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 125.4 KB 125.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.6 KB | Display | ![]() |
Images | ![]() | 95.4 KB | ||
Filedesc metadata | ![]() | 17 KB | ||
Others | ![]() ![]() | 202.3 MB 202.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 21.2 KB | Display | |
Data in CIF | ![]() | 28.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6c4iMC ![]() 7340C ![]() 6c4hC ![]() 6c5lC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | non-stop termination complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: non-stop termination complex, half map #1
File | emd_7341_half_map_1.map | ||||||||||||
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Annotation | non-stop termination complex, half map #1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: non-stop termination complex, half map #2
File | emd_7341_half_map_2.map | ||||||||||||
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Annotation | non-stop termination complex, half map #2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : nonstop ribosomal complex with ArfA/RF2
+Supramolecule #1: nonstop ribosomal complex with ArfA/RF2
+Supramolecule #2: 50S subunit
+Supramolecule #3: 30S subunit
+Supramolecule #11: 30S ribosomal proteins
+Supramolecule #12: 50S ribosomal proteins
+Supramolecule #4: Peptide chain release factor 2
+Supramolecule #5: Alternative ribosome-rescue factor A
+Supramolecule #6: E-site or P-site tRNA fMet
+Supramolecule #7: nonstop mRNA
+Supramolecule #8: 23S rRNA
+Supramolecule #9: 5S rRNA
+Supramolecule #10: 16S rRNA
+Supramolecule #13: 50S ribosomal protein L2
+Supramolecule #14: 50S ribosomal protein L3
+Supramolecule #15: 50S ribosomal protein L4
+Supramolecule #16: 50S ribosomal protein L5
+Supramolecule #17: 50S ribosomal protein L6
+Supramolecule #18: 50S ribosomal protein L9
+Supramolecule #19: 50S ribosomal protein L10
+Supramolecule #20: 50S ribosomal protein L11
+Supramolecule #21: 50S ribosomal protein L13
+Supramolecule #22: 50S ribosomal protein L14
+Supramolecule #23: 50S ribosomal protein L15
+Supramolecule #24: 50S ribosomal protein L16
+Supramolecule #25: 50S ribosomal protein L17
+Supramolecule #26: 50S ribosomal protein L18
+Supramolecule #27: 50S ribosomal protein L19
+Supramolecule #28: 50S ribosomal protein L20
+Supramolecule #29: 50S ribosomal protein L21
+Supramolecule #30: 50S ribosomal protein L22
+Supramolecule #31: 50S ribosomal protein L23
+Supramolecule #32: 50S ribosomal protein L24
+Supramolecule #33: 50S ribosomal protein L25
+Supramolecule #34: 50S ribosomal protein L27
+Supramolecule #35: 50S ribosomal protein L28
+Supramolecule #36: 50S ribosomal protein L29
+Supramolecule #37: 50S ribosomal protein L30
+Supramolecule #38: 50S ribosomal protein L31
+Supramolecule #39: 50S ribosomal protein L32
+Supramolecule #40: 50S ribosomal protein L33
+Supramolecule #41: 50S ribosomal protein L34
+Supramolecule #42: 50S ribosomal protein L35
+Supramolecule #43: 50S ribosomal protein L36
+Supramolecule #44: 30S ribosomal protein S2
+Supramolecule #45: 30S ribosomal protein S3
+Supramolecule #46: 30S ribosomal protein S4
+Supramolecule #47: 30S ribosomal protein S5
+Supramolecule #48: 30S ribosomal protein S6
+Supramolecule #49: 30S ribosomal protein S7
+Supramolecule #50: 30S ribosomal protein S8
+Supramolecule #51: 30S ribosomal protein S9
+Supramolecule #52: 30S ribosomal protein S10
+Supramolecule #53: 30S ribosomal protein S11
+Supramolecule #54: 30S ribosomal protein S12
+Supramolecule #55: 30S ribosomal protein S13
+Supramolecule #56: 30S ribosomal protein S14
+Supramolecule #57: 30S ribosomal protein S15
+Supramolecule #58: 30S ribosomal protein S16
+Supramolecule #59: 30S ribosomal protein S17
+Supramolecule #60: 30S ribosomal protein S18
+Supramolecule #61: 30S ribosomal protein S19
+Supramolecule #62: 30S ribosomal protein S20
+Supramolecule #63: 30S ribosomal protein S21
+Macromolecule #1: 23S rRNA
+Macromolecule #2: 5S rRNA
+Macromolecule #34: 16S rRNA
+Macromolecule #57: E-site or P-site tRNA fMet
+Macromolecule #58: mRNA
+Macromolecule #3: 50S ribosomal protein L2
+Macromolecule #4: 50S ribosomal protein L3
+Macromolecule #5: 50S ribosomal protein L4
+Macromolecule #6: 50S ribosomal protein L5
+Macromolecule #7: 50S ribosomal protein L6
+Macromolecule #8: 50S ribosomal protein L9
+Macromolecule #9: 50S ribosomal protein L10
+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 L31
+Macromolecule #29: 50S ribosomal protein L32
+Macromolecule #30: 50S ribosomal protein L33
+Macromolecule #31: 50S ribosomal protein L34
+Macromolecule #32: 50S ribosomal protein L35
+Macromolecule #33: 50S ribosomal protein L36
+Macromolecule #35: 30S ribosomal protein S2
+Macromolecule #36: 30S ribosomal protein S3
+Macromolecule #37: 30S ribosomal protein S4
+Macromolecule #38: 30S ribosomal protein S5
+Macromolecule #39: 30S ribosomal protein S6
+Macromolecule #40: 30S ribosomal protein S7
+Macromolecule #41: 30S ribosomal protein S8
+Macromolecule #42: 30S ribosomal protein S9
+Macromolecule #43: 30S ribosomal protein S10
+Macromolecule #44: 30S ribosomal protein S11
+Macromolecule #45: 30S ribosomal protein S12
+Macromolecule #46: 30S ribosomal protein S13
+Macromolecule #47: 30S ribosomal protein S14
+Macromolecule #48: 30S ribosomal protein S15
+Macromolecule #49: 30S ribosomal protein S16
+Macromolecule #50: 30S ribosomal protein S17
+Macromolecule #51: 30S ribosomal protein S18
+Macromolecule #52: 30S ribosomal protein S19
+Macromolecule #53: 30S ribosomal protein S20
+Macromolecule #54: 30S ribosomal protein S21
+Macromolecule #55: Peptide chain release factor 2
+Macromolecule #56: Alternative ribosome-rescue factor A
+Macromolecule #59: MAGNESIUM ION
+Macromolecule #60: ZINC ION
+Macromolecule #61: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 Component:
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Grid | Model: C-flat-2/0.5 4C / Pretreatment - Type: GLOW DISCHARGE | |||||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: Grids were blotted for 3.5 seconds.. |
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Electron microscopy
Microscope | JEOL 3200FS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 20.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated magnification: 83822 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Sample stage | Cooling holder cryogen: NITROGEN |