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- EMDB-12734: Cryo-EM structure of a Bacillus subtilis MifM-stalled ribosome-na... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-12734 | |||||||||
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Title | Cryo-EM structure of a Bacillus subtilis MifM-stalled ribosome-nascent chain complex with (p)ppGpp-SRP bound | |||||||||
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![]() | signal recognition particle co-translational targeting alarmones translation GTPases stress response / RIBOSOME | |||||||||
Function / homology | ![]() signal recognition particle / signal-recognition-particle GTPase / 7S RNA binding / positive regulation of rRNA processing / SRP-dependent cotranslational protein targeting to membrane / nucleoid / rRNA processing / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis ...signal recognition particle / signal-recognition-particle GTPase / 7S RNA binding / positive regulation of rRNA processing / SRP-dependent cotranslational protein targeting to membrane / nucleoid / rRNA processing / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / small ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / response to antibiotic / GTPase activity / mRNA binding / GTP binding / ATP hydrolysis activity / DNA binding / RNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.33 Å | |||||||||
![]() | Kratzat H / Czech L | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp. Authors: Laura Czech / Christopher-Nils Mais / Hanna Kratzat / Pinku Sarmah / Pietro Giammarinaro / Sven-Andreas Freibert / Hanna Folke Esser / Joanna Musial / Otto Berninghausen / Wieland Steinchen ...Authors: Laura Czech / Christopher-Nils Mais / Hanna Kratzat / Pinku Sarmah / Pietro Giammarinaro / Sven-Andreas Freibert / Hanna Folke Esser / Joanna Musial / Otto Berninghausen / Wieland Steinchen / Roland Beckmann / Hans-Georg Koch / Gert Bange / ![]() Abstract: The stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known ...The stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known as (p)ppGpp. Here, we report that (p)ppGpp inhibits the signal recognition particle (SRP)-dependent protein targeting pathway, which is essential for membrane protein biogenesis and protein secretion. More specifically, (p)ppGpp binds to the SRP GTPases Ffh and FtsY, and inhibits the formation of the SRP receptor-targeting complex, which is central for the coordinated binding of the translating ribosome to the SecYEG translocon. Cryo-EM analysis of SRP bound to translating ribosomes suggests that (p)ppGpp may induce a distinct conformational stabilization of the NG domain of Ffh and FtsY in Bacillus subtilis but not in E. coli. | |||||||||
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 | ![]() | 89.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 71.6 KB 71.6 KB | Display Display | ![]() |
Images | ![]() | 73.9 KB | ||
Filedesc metadata | ![]() | 13.8 KB | ||
Others | ![]() ![]() | 22.2 MB 168.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7o5bMC ![]() 7o9fC ![]() 7o9gC ![]() 7o9hC ![]() 7o9iC M: atomic model generated by this map C: citing same article ( |
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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
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.059 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: #2
File | emd_12734_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #1
File | emd_12734_additional_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : SRP-bound MifM-stalled ribosome nascent chain complex
+Supramolecule #1: SRP-bound MifM-stalled ribosome nascent chain complex
+Macromolecule #1: tRNA
+Macromolecule #2: mRNA
+Macromolecule #3: SRP RNA (266-MER)
+Macromolecule #8: 23S rRNA (2887-MER)
+Macromolecule #9: 5S rRNA (112-MER)
+Macromolecule #37: 16S rRNA (1533-MER)
+Macromolecule #4: Signal recognition particle protein
+Macromolecule #5: MifM-stalling construct
+Macromolecule #6: 50S ribosomal protein L10
+Macromolecule #7: 50S ribosomal protein L11
+Macromolecule #10: 50S ribosomal protein L2
+Macromolecule #11: 50S ribosomal protein L3
+Macromolecule #12: 50S ribosomal protein L4
+Macromolecule #13: 50S ribosomal protein L5
+Macromolecule #14: 50S ribosomal protein L6
+Macromolecule #15: 50S ribosomal protein L13
+Macromolecule #16: 50S ribosomal protein L14
+Macromolecule #17: 50S ribosomal protein L15
+Macromolecule #18: 50S ribosomal protein L16
+Macromolecule #19: 50S ribosomal protein L17
+Macromolecule #20: 50S ribosomal protein L18
+Macromolecule #21: 50S ribosomal protein L19
+Macromolecule #22: 50S ribosomal protein L20
+Macromolecule #23: 50S ribosomal protein L21
+Macromolecule #24: 50S ribosomal protein L22
+Macromolecule #25: 50S ribosomal protein L23
+Macromolecule #26: 50S ribosomal protein L24
+Macromolecule #27: 50S ribosomal protein L27
+Macromolecule #28: 50S ribosomal protein L28
+Macromolecule #29: 50S ribosomal protein L29
+Macromolecule #30: 50S ribosomal protein L30
+Macromolecule #31: 50S ribosomal protein L32
+Macromolecule #32: 50S ribosomal protein L33 1
+Macromolecule #33: 50S ribosomal protein L34
+Macromolecule #34: 50S ribosomal protein L35
+Macromolecule #35: 50S ribosomal protein L36
+Macromolecule #36: 50S ribosomal protein L31
+Macromolecule #38: 30S ribosomal protein S2
+Macromolecule #39: 30S ribosomal protein S3
+Macromolecule #40: 30S ribosomal protein S4
+Macromolecule #41: 30S ribosomal protein S5
+Macromolecule #42: 30S ribosomal protein S6
+Macromolecule #43: 30S ribosomal protein S7
+Macromolecule #44: 30S ribosomal protein S8
+Macromolecule #45: 30S ribosomal protein S9
+Macromolecule #46: 30S ribosomal protein S10
+Macromolecule #47: 30S ribosomal protein S11
+Macromolecule #48: 30S ribosomal protein S12
+Macromolecule #49: 30S ribosomal protein S13
+Macromolecule #50: 30S ribosomal protein S14
+Macromolecule #51: 30S ribosomal protein S15
+Macromolecule #52: 30S ribosomal protein S16
+Macromolecule #53: 30S ribosomal protein S17
+Macromolecule #54: 30S ribosomal protein S18
+Macromolecule #55: 30S ribosomal protein S19
+Macromolecule #56: 30S ribosomal protein S20
+Macromolecule #57: GUANOSINE-5',3'-TETRAPHOSPHATE
-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 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 25.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.33 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 21229 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |