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- EMDB-4300: Structure of a prehandover mammalian ribosomal SRP and SRP recept... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-4300 | |||||||||
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Title | Structure of a prehandover mammalian ribosomal SRP and SRP receptor targeting complex | |||||||||
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![]() | ER membrane targeting ribosome Signal recognition particle / TRANSLATION | |||||||||
Function / homology | ![]() SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / signal recognition particle binding / granulocyte differentiation / protein targeting to ER / signal-recognition-particle GTPase / protein localization to Golgi apparatus ...SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / signal recognition particle binding / granulocyte differentiation / protein targeting to ER / signal-recognition-particle GTPase / protein localization to Golgi apparatus / negative regulation of translational elongation / SRP-dependent cotranslational protein targeting to membrane, translocation / 7S RNA binding / Golgi to plasma membrane protein transport / SRP-dependent cotranslational protein targeting to membrane / exocrine pancreas development / TPR domain binding / ribonucleoprotein complex binding / cytoplasmic microtubule / neutrophil chemotaxis / intracellular protein transport / GDP binding / ribosome binding / nuclear speck / GTPase activity / endoplasmic reticulum membrane / GTP binding / nucleolus / endoplasmic reticulum / Golgi apparatus / ATP hydrolysis activity / nucleoplasm / nucleus / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
![]() | Kobayashi K / Jomaa A | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex. Authors: Kan Kobayashi / Ahmad Jomaa / Jae Ho Lee / Sowmya Chandrasekar / Daniel Boehringer / Shu-Ou Shan / Nenad Ban / ![]() ![]() Abstract: Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER ...Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER membrane followed by the transfer of the signal sequence to the translocon. Here, we present the cryo-electron microscopy structure of the mammalian translating ribosome in complex with SRP and SR in a conformation preceding signal sequence handover. The structure visualizes all eukaryotic-specific SRP and SR proteins and reveals their roles in stabilizing this conformation by forming a large protein assembly at the distal site of SRP RNA. We provide biochemical evidence that the guanosine triphosphate hydrolysis of SRP·SR is delayed at this stage, possibly to provide a time window for signal sequence handover to the translocon. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
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Downloads & links
-EMDB archive
Map data | ![]() | 116.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 89 KB 89 KB | Display Display | ![]() |
Images | ![]() | 265.7 KB | ||
Filedesc metadata | ![]() | 17.2 KB | ||
Others | ![]() ![]() | 98 MB 98.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 14 KB | Display | |
Data in CIF | ![]() | 16.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6frkMC 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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Voxel size | X=Y=Z: 1.39 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : Translating ribosome bound to SRP and SRP receptor
+Supramolecule #1: Translating ribosome bound to SRP and SRP receptor
+Supramolecule #2: Ribosome
+Supramolecule #3: SRP
+Supramolecule #4: SRP receptor
+Supramolecule #5: Signal sequence
+Macromolecule #1: Canis lupus familiaris RNA, 7SL, cytoplasmic 1 (RN7SL1), SRP RNA
+Macromolecule #2: tRNA
+Macromolecule #5: 28S ribosomal RNA
+Macromolecule #7: 5S ribosomal RNA
+Macromolecule #8: 5.8S ribosomal RNA
+Macromolecule #3: Ribosomal protein eL28
+Macromolecule #4: Ribosomal protein L12
+Macromolecule #6: 60S acidic ribosomal protein P0
+Macromolecule #9: Ribosomal protein L8
+Macromolecule #10: Ribosomal protein uL3
+Macromolecule #11: Ribosomal protein uL4
+Macromolecule #12: Ribosomal protein uL18
+Macromolecule #13: Ribosomal protein eL6
+Macromolecule #14: Ribosomal protein uL30
+Macromolecule #15: Ribosomal protein eL8
+Macromolecule #16: Ribosomal protein uL6
+Macromolecule #17: Ribosomal protein uL16
+Macromolecule #18: Ribosomal protein uL5
+Macromolecule #19: Ribosomal protein eL13
+Macromolecule #20: Ribosomal protein eL14
+Macromolecule #21: Ribosomal protein L15
+Macromolecule #22: Ribosomal protein uL13
+Macromolecule #23: Ribosomal protein uL22
+Macromolecule #24: Ribosomal protein eL18
+Macromolecule #25: Ribosomal protein eL19
+Macromolecule #26: Ribosomal protein eL20
+Macromolecule #27: Ribosomal protein eL21
+Macromolecule #28: Ribosomal protein eL22
+Macromolecule #29: Ribosomal protein L23
+Macromolecule #30: Ribosomal protein eL24
+Macromolecule #31: Ribosomal protein uL23
+Macromolecule #32: Ribosomal protein uL24
+Macromolecule #33: 60S ribosomal protein L27
+Macromolecule #34: Ribosomal protein uL15
+Macromolecule #35: 60S ribosomal protein L29
+Macromolecule #36: Ribosomal protein eL30
+Macromolecule #37: Ribosomal protein eL31
+Macromolecule #38: Ribosomal protein eL32
+Macromolecule #39: Ribosomal protein eL33
+Macromolecule #40: Ribosomal protein eL34
+Macromolecule #41: Ribosomal protein uL29
+Macromolecule #42: Ribosomal protein eL36
+Macromolecule #43: Ribosomal protein L37
+Macromolecule #44: Ribosomal protein eL38
+Macromolecule #45: Ribosomal protein eL39
+Macromolecule #46: Ribosomal protein eL40
+Macromolecule #47: Ribosomal protein eL41
+Macromolecule #48: Ribosomal protein eL42
+Macromolecule #49: Ribosomal protein eL43
+Macromolecule #50: Signal recognition particle subunit SRP19
+Macromolecule #51: Signal recognition particle subunit SRP72,Signal recognition part...
+Macromolecule #52: Signal sequence
+Macromolecule #53: Signal recognition particle subunit SRP68
+Macromolecule #54: SRP receptor beta subunit
+Macromolecule #55: Signal recognition particle 9 kDa protein
+Macromolecule #56: Signal recognition particle 54 kDa protein
+Macromolecule #57: SRP receptor alpha subunit
+Macromolecule #58: Signal recognition particle 14 kDa protein
+Macromolecule #59: MAGNESIUM ION
+Macromolecule #60: ZINC ION
+Macromolecule #61: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #62: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
-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: 7.6 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON |
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: RECIPROCAL / Protocol: RIGID BODY FIT |
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Output model | ![]() PDB-6frk: |