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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-14191 | |||||||||
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Title | Ternary complex of ribosome nascent chain with SRP and NAC | |||||||||
![]() | Ternary ribosome-nascent chain, SRP and NAC complex | |||||||||
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![]() | Ribosome / SRP / NAC / nascent chain / co-translational / Endoplasmic reticulum / co-translational protein targeting / co-translational folding | |||||||||
Function / homology | ![]() PI3K Cascade / PIP3 activates AKT signaling / FLT3 Signaling / Negative regulation of FLT3 / FLT3 signaling through SRC family kinases / RAF/MAP kinase cascade / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development ...PI3K Cascade / PIP3 activates AKT signaling / FLT3 Signaling / Negative regulation of FLT3 / FLT3 signaling through SRC family kinases / RAF/MAP kinase cascade / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / positive regulation of cell proliferation involved in heart morphogenesis / endoplasmic reticulum signal peptide binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / signal recognition particle, endoplasmic reticulum targeting / Major pathway of rRNA processing in the nucleolus and cytosol / GTP hydrolysis and joining of the 60S ribosomal subunit / positive regulation of skeletal muscle tissue growth / cardiac ventricle development / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / granulocyte differentiation / signal recognition particle binding / signal recognition particle / cotranslational protein targeting to membrane / protein targeting to ER / signal-recognition-particle GTPase / dendritic cell differentiation / SRP-dependent cotranslational protein targeting to membrane, translocation / heart trabecula morphogenesis / 7S RNA binding / skeletal muscle tissue regeneration / SRP-dependent cotranslational protein targeting to membrane / exocrine pancreas development / ribosomal subunit / embryonic hemopoiesis / exit from mitosis / optic nerve development / retinal ganglion cell axon guidance / positive regulation of signal transduction by p53 class mediator / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane / ribonucleoprotein complex binding / protein-RNA complex assembly / rough endoplasmic reticulum / MDM2/MDM4 family protein binding / neutrophil chemotaxis / B cell differentiation / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / cytokine activity / wound healing / receptor tyrosine kinase binding / antimicrobial humoral immune response mediated by antimicrobial peptide / GDP binding / protein transport / regulation of translation / large ribosomal subunit / retina development in camera-type eye / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / defense response to Gram-negative bacterium / killing of cells of another organism / cytosolic large ribosomal subunit / in utero embryonic development / cytoplasmic translation / transcription coactivator activity / tRNA binding / postsynaptic density / rRNA binding / nuclear speck / nuclear body / ribosome / structural constituent of ribosome / protein domain specific binding / translation / response to xenobiotic stimulus / ribonucleoprotein complex / focal adhesion / GTPase activity / mRNA binding / positive regulation of cell population proliferation / synapse / GTP binding / nucleolus / negative regulation of transcription by RNA polymerase II / cell surface / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / extracellular space / RNA binding / extracellular exosome / zinc ion binding / nucleus Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.83 Å | |||||||||
![]() | Jomaa A / Gamerdinger M / Hsieh H / Wallisch A / Chandrasekaran V / Ulusoy Z / Scaiola A / Hegde R / Shan S / Ban N / Deuerling E | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting. Authors: Ahmad Jomaa / Martin Gamerdinger / Hao-Hsuan Hsieh / Annalena Wallisch / Viswanathan Chandrasekaran / Zeynel Ulusoy / Alain Scaiola / Ramanujan S Hegde / Shu-Ou Shan / Nenad Ban / Elke Deuerling / ![]() ![]() ![]() ![]() Abstract: The nascent polypeptide-associated complex (NAC) interacts with newly synthesized proteins at the ribosomal tunnel exit and competes with the signal recognition particle (SRP) to prevent mistargeting ...The nascent polypeptide-associated complex (NAC) interacts with newly synthesized proteins at the ribosomal tunnel exit and competes with the signal recognition particle (SRP) to prevent mistargeting of cytosolic and mitochondrial polypeptides to the endoplasmic reticulum (ER). How NAC antagonizes SRP and how this is overcome by ER targeting signals are unknown. Here, we found that NAC uses two domains with opposing effects to control SRP access. The core globular domain prevented SRP from binding to signal-less ribosomes, whereas a flexibly attached domain transiently captured SRP to permit scanning of nascent chains. The emergence of an ER-targeting signal destabilized NAC's globular domain and facilitated SRP access to the nascent chain. These findings elucidate how NAC hands over the signal sequence to SRP and imparts specificity of protein localization. | |||||||||
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 | ![]() | 321.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 78.7 KB 78.7 KB | Display Display | ![]() |
Images | ![]() | 173.5 KB | ||
Filedesc metadata | ![]() | 16.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7qwqMC ![]() 7qwrC ![]() 7qwsC 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
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Ternary ribosome-nascent chain, SRP and NAC complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 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 : Ternary ribosome-nascent chain SRP NAC complex
+Supramolecule #1: Ternary ribosome-nascent chain SRP NAC complex
+Supramolecule #2: Ribosome
+Supramolecule #3: SRP RNA 7SL
+Supramolecule #4: Signal recognition particle proteins
+Supramolecule #5: Nascent chain preprolactin
+Supramolecule #6: Isoform 2 of Transcription factor BTF3
+Macromolecule #1: SRP RNA 7SL
+Macromolecule #9: 28S rRNA
+Macromolecule #47: 5S ribosomal RNA
+Macromolecule #49: 5.8S ribosomal RNA
+Macromolecule #2: Signal recognition particle 19 kDa protein
+Macromolecule #3: Nascent chain preprolactin
+Macromolecule #4: Isoform 2 of Transcription factor BTF3
+Macromolecule #5: Signal recognition particle subunit SRP68
+Macromolecule #6: Signal recognition particle 54 kDa protein
+Macromolecule #7: L8
+Macromolecule #8: 60S ribosomal protein L29
+Macromolecule #10: uL3
+Macromolecule #11: 60S ribosomal protein L30
+Macromolecule #12: 60S ribosomal protein L4
+Macromolecule #13: Ribosomal protein L31
+Macromolecule #14: Ribosomal_L18_c domain-containing protein
+Macromolecule #15: Ribosomal protein L32
+Macromolecule #16: 60S ribosomal protein L6
+Macromolecule #17: 60S ribosomal protein L35a
+Macromolecule #18: uL30
+Macromolecule #19: 60S ribosomal protein L34
+Macromolecule #20: 60S ribosomal protein L7a
+Macromolecule #21: 60S ribosomal protein L35
+Macromolecule #22: 60S ribosomal protein L9
+Macromolecule #23: 60S ribosomal protein L36
+Macromolecule #24: 60S ribosomal protein L10
+Macromolecule #25: Ribosomal protein L37
+Macromolecule #26: Ribosomal protein L11
+Macromolecule #27: 60S ribosomal protein L38
+Macromolecule #28: 60S ribosomal protein L13
+Macromolecule #29: Ribosomal protein L39
+Macromolecule #30: 60S ribosomal protein L14
+Macromolecule #31: Ubiquitin A-52 residue ribosomal protein fusion product 1
+Macromolecule #32: Ribosomal protein L15
+Macromolecule #33: 60s ribosomal protein l41
+Macromolecule #34: 60S ribosomal protein L13a
+Macromolecule #35: eL42
+Macromolecule #36: 60S ribosomal protein L17
+Macromolecule #37: eL43
+Macromolecule #38: eL18
+Macromolecule #39: 60S ribosomal protein L28
+Macromolecule #40: 60S ribosomal protein L19
+Macromolecule #41: 60S ribosomal protein L18a
+Macromolecule #42: 60S ribosomal protein L21
+Macromolecule #43: Ribosomal protein L22
+Macromolecule #44: Ribosomal protein L23
+Macromolecule #45: Ribosomal protein L24
+Macromolecule #46: Ribosomal_L23eN domain-containing protein
+Macromolecule #48: Ribosomal protein L26
+Macromolecule #50: 60S ribosomal protein L27
+Macromolecule #51: 60S ribosomal protein L27a
+Macromolecule #52: Nascent polypeptide-associated complex subunit alpha
+Macromolecule #53: MAGNESIUM ION
+Macromolecule #54: ZINC ION
-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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Grid | Model: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. |
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 95 % / 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: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.83 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 51843 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |