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Yorodumi- EMDB-0270: Stringent response control by a bifunctional RelA enzyme in the p... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0270 | |||||||||
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Title | Stringent response control by a bifunctional RelA enzyme in the presence and absence of the ribosome | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Structure of bifunctional Rel on B. subtilis 70S / ribosome | |||||||||
Function / homology | Function and homology information GTP diphosphokinase / GTP diphosphokinase activity / guanosine tetraphosphate biosynthetic process / positive regulation of rRNA processing / nucleoid / rRNA processing / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / kinase activity ...GTP diphosphokinase / GTP diphosphokinase activity / guanosine tetraphosphate biosynthetic process / positive regulation of rRNA processing / nucleoid / rRNA processing / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / kinase activity / 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 / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / response to antibiotic / mRNA binding / GTP binding / DNA binding / RNA binding / zinc ion binding / ATP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Bacillus subtilis subsp. subtilis str. 168 (bacteria) / Bacillus subtilis (strain 168) (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
Authors | Wilson DN / Abdelshahid M | |||||||||
Citation | Journal: Cell Rep / Year: 2020 Title: Structural Basis for Regulation of the Opposing (p)ppGpp Synthetase and Hydrolase within the Stringent Response Orchestrator Rel. Authors: Patrick Pausch / Maha Abdelshahid / Wieland Steinchen / Heinrich Schäfer / Fabio Lino Gratani / Sven-Andreas Freibert / Christiane Wolz / Kürşad Turgay / Daniel N Wilson / Gert Bange / Abstract: The stringent response enables metabolic adaptation of bacteria under stress conditions and is governed by RelA/SpoT Homolog (RSH)-type enzymes. Long RSH-type enzymes encompass an N-terminal domain ...The stringent response enables metabolic adaptation of bacteria under stress conditions and is governed by RelA/SpoT Homolog (RSH)-type enzymes. Long RSH-type enzymes encompass an N-terminal domain (NTD) harboring the second messenger nucleotide (p)ppGpp hydrolase and synthetase activity and a stress-perceiving and regulatory C-terminal domain (CTD). CTD-mediated binding of Rel to stalled ribosomes boosts (p)ppGpp synthesis. However, how the opposing activities of the NTD are controlled in the absence of stress was poorly understood. Here, we demonstrate on the RSH-type protein Rel that the critical regulative elements reside within the TGS (ThrRS, GTPase, and SpoT) subdomain of the CTD, which associates to and represses the synthetase to concomitantly allow for activation of the hydrolase. Furthermore, we show that Rel forms homodimers, which appear to control the interaction with deacylated-tRNA, but not the enzymatic activity of Rel. Collectively, our study provides a detailed molecular view into the mechanism of stringent response repression in the absence of stress. | |||||||||
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_0270.map.gz | 104.7 MB | EMDB map data format | |
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Header (meta data) | emd-0270-v30.xml emd-0270.xml | 74.5 KB 74.5 KB | Display Display | EMDB header |
Images | emd_0270.png | 66 KB | ||
Filedesc metadata | emd-0270.cif.gz | 13.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0270 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0270 | HTTPS FTP |
-Validation report
Summary document | emd_0270_validation.pdf.gz | 495 KB | Display | EMDB validaton report |
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Full document | emd_0270_full_validation.pdf.gz | 494.6 KB | Display | |
Data in XML | emd_0270_validation.xml.gz | 6.9 KB | Display | |
Data in CIF | emd_0270_validation.cif.gz | 8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0270 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0270 | HTTPS FTP |
-Related structure data
Related structure data | 6htqMC 6yxaC 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_0270.map.gz / Format: CCP4 / Size: 178 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 : Bacillus subtilis subsp. subtilis str. 168
+Supramolecule #1: Bacillus subtilis subsp. subtilis str. 168
+Macromolecule #1: 23S ribosomal RNA
+Macromolecule #2: 5S ribosomal RNA
+Macromolecule #30: 16S rRNA
+Macromolecule #50: P-tRNA
+Macromolecule #52: A/R-tRNA
+Macromolecule #53: E-tRNA
+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 L13
+Macromolecule #9: 50S ribosomal protein L14
+Macromolecule #10: 50S ribosomal protein L15
+Macromolecule #11: 50S ribosomal protein L16
+Macromolecule #12: 50S ribosomal protein L17
+Macromolecule #13: 50S ribosomal protein L18
+Macromolecule #14: 50S ribosomal protein L19
+Macromolecule #15: 50S ribosomal protein L20
+Macromolecule #16: 50S ribosomal protein L21
+Macromolecule #17: 50S ribosomal protein L22
+Macromolecule #18: 50S ribosomal protein L23
+Macromolecule #19: 50S ribosomal protein L24
+Macromolecule #20: 50S ribosomal protein L27
+Macromolecule #21: 50S ribosomal protein L28
+Macromolecule #22: 50S ribosomal protein L29
+Macromolecule #23: 50S ribosomal protein L30
+Macromolecule #24: 50S ribosomal protein L32
+Macromolecule #25: 50S ribosomal protein L33 1
+Macromolecule #26: 50S ribosomal protein L34
+Macromolecule #27: 50S ribosomal protein L35
+Macromolecule #28: 50S ribosomal protein L36
+Macromolecule #29: 50S ribosomal protein L31
+Macromolecule #31: 30S ribosomal protein S2
+Macromolecule #32: 30S ribosomal protein S3
+Macromolecule #33: 30S ribosomal protein S4
+Macromolecule #34: 30S ribosomal protein S5
+Macromolecule #35: 30S ribosomal protein S6
+Macromolecule #36: 30S ribosomal protein S7
+Macromolecule #37: 30S ribosomal protein S8
+Macromolecule #38: 30S ribosomal protein S9
+Macromolecule #39: 30S ribosomal protein S10
+Macromolecule #40: 30S ribosomal protein S11
+Macromolecule #41: 30S ribosomal protein S12
+Macromolecule #42: 30S ribosomal protein S13
+Macromolecule #43: 30S ribosomal protein S14
+Macromolecule #44: 30S ribosomal protein S15
+Macromolecule #45: 30S ribosomal protein S16
+Macromolecule #46: 30S ribosomal protein S17
+Macromolecule #47: 30S ribosomal protein S18
+Macromolecule #48: 30S ribosomal protein S19
+Macromolecule #49: 30S ribosomal protein S20
+Macromolecule #51: GTP pyrophosphokinase
-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
Startup model | Type of model: EMDB MAP |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 650054 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |