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- PDB-2go5: Structure of signal recognition particle receptor (SR) in complex... -
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Basic information
Entry | Database: PDB / ID: 2go5 | ||||||
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Title | Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex | ||||||
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![]() | TRANSLATION/RNA / SR / SRP / RIBOSOME / TRANSLATION-RNA COMPLEX | ||||||
Function / homology | ![]() SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / signal recognition particle, endoplasmic reticulum targeting / granulocyte differentiation / signal recognition particle binding / cotranslational protein targeting to membrane / endoplasmic reticulum signal peptide binding / signal-recognition-particle GTPase / protein targeting to ER ...SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / signal recognition particle, endoplasmic reticulum targeting / granulocyte differentiation / signal recognition particle binding / cotranslational protein targeting to membrane / endoplasmic reticulum signal peptide binding / signal-recognition-particle GTPase / protein targeting to ER / XBP1(S) activates chaperone genes / SRP-dependent cotranslational protein targeting to membrane / 7S RNA binding / exocrine pancreas development / SRP-dependent cotranslational protein targeting to membrane, translocation / cytoplasmic microtubule / SRP-dependent cotranslational protein targeting to membrane / vesicle-mediated transport / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / neutrophil chemotaxis / chloroplast / intracellular protein transport / GDP binding / cytosolic large ribosomal subunit / cytoplasmic translation / rRNA binding / nuclear speck / structural constituent of ribosome / translation / GTPase activity / mRNA binding / ubiquitin protein ligase binding / endoplasmic reticulum membrane / GTP binding / Golgi apparatus / endoplasmic reticulum / ATP hydrolysis activity / RNA binding / extracellular exosome / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.4 Å | ||||||
![]() | Halic, M. / Gartmann, M. / Schlenker, O. / Mielke, T. / Pool, M.R. / Sinning, I. / Beckmann, R. | ||||||
![]() | ![]() Title: Signal recognition particle receptor exposes the ribosomal translocon binding site. Authors: Mario Halic / Marco Gartmann / Oliver Schlenker / Thorsten Mielke / Martin R Pool / Irmgard Sinning / Roland Beckmann / ![]() Abstract: Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by ...Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted. | ||||||
History |
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Remark 999 | SEQUENCE Residue (A G 124) and Residue (A G 125) are not linked. Distance of O3*-P bond is 4.22. ...SEQUENCE Residue (A G 124) and Residue (A G 125) are not linked. Distance of O3*-P bond is 4.22. Residue (A C 221) and Residue (A G 222) are not linked. Distance of O3*-P bond is 3.26. Residue (1 SER 0) and Residue (1 MET 1) are not linked. Distance of C-N bond is 17.58. Residue (1 GLY 27) and Residue (1 PRO 28) are not linked. Distance of C-N bond is 7.21. Residue (1 LEU 52) and Residue (1 THR 53) are not linked. Distance of C-N bond is 5.58. |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 281.6 KB | Display | ![]() |
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PDB format | ![]() | 220 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 841.4 KB | Display | ![]() |
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Full document | ![]() | 913 KB | Display | |
Data in XML | ![]() | 41.7 KB | Display | |
Data in CIF | ![]() | 61.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1217MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-RNA chain , 2 types, 2 molecules A9
#1: RNA chain | Mass: 41199.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: RNA chain | Mass: 29170.479 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Signal recognition particle ... , 4 types, 4 molecules BW12
#3: Protein | Mass: 12561.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#4: Protein | Mass: 12473.440 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#5: Protein | Mass: 21329.512 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
#6: Protein | Mass: 23536.982 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Ribosomal protein ... , 3 types, 3 molecules 546
#7: Protein | Mass: 14401.041 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#8: Protein | Mass: 16920.203 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#9: Protein | Mass: 14152.365 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: SR-SRP-RNC COMPLEX / Type: RIBOSOME |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: CARBON |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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Microscopy | Model: FEI TECNAI F30 |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 800 nm |
Image recording | Film or detector model: KODAK SO-163 FILM |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
Radiation wavelength | Relative weight: 1 |
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Processing
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||
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3D reconstruction | Resolution: 7.4 Å / Resolution method: FSC 0.5 CUT-OFF / Symmetry type: POINT | ||||||||||||
Refinement | Highest resolution: 7.4 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 7.4 Å
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