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Open data
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Basic information
| Entry | Database: PDB / ID: 7qwq | ||||||
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| Title | Ternary complex of ribosome nascent chain with SRP and NAC | ||||||
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Keywords | RIBOSOME / SRP / NAC / nascent chain / co-translational / Endoplasmic reticulum / co-translational protein targeting / co-translational folding | ||||||
| Function / homology | Function and homology informationPI3K Cascade / PIP3 activates AKT signaling / FLT3 Signaling / FLT3 signaling through SRC family kinases / RAF/MAP kinase cascade / Negative regulation of FLT3 / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / endoplasmic reticulum signal sequence receptor activity / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / negative regulation of striated muscle cell apoptotic process ...PI3K Cascade / PIP3 activates AKT signaling / FLT3 Signaling / FLT3 signaling through SRC family kinases / RAF/MAP kinase cascade / Negative regulation of FLT3 / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / endoplasmic reticulum signal sequence receptor activity / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / negative regulation of striated muscle cell apoptotic process / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / Major pathway of rRNA processing in the nucleolus and cytosol / GTP hydrolysis and joining of the 60S ribosomal subunit / signal recognition particle, endoplasmic reticulum targeting / regulation of skeletal muscle fiber development / granulocyte differentiation / positive regulation of cell proliferation involved in heart morphogenesis / positive regulation of skeletal muscle tissue growth / 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) / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / signal recognition particle / cardiac ventricle development / signal recognition particle binding / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / cotranslational protein targeting to membrane / exocrine pancreas development / signal-recognition-particle GTPase / heart trabecula morphogenesis / dendritic cell differentiation / protein targeting to ER / SRP-dependent cotranslational protein targeting to membrane, translocation / 7S RNA binding / skeletal muscle tissue regeneration / SRP-dependent cotranslational protein targeting to membrane / embryonic hemopoiesis / ribonucleoprotein complex binding / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane / positive regulation of signal transduction by p53 class mediator / neutrophil chemotaxis / B cell differentiation / protein-RNA complex assembly / rough endoplasmic reticulum / MDM2/MDM4 family protein binding / cytokine activity / wound healing / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Dengue Virus Genome Translation and Replication / receptor tyrosine kinase binding / GDP binding / protein transport / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit rRNA binding / killing of cells of another organism / defense response to Gram-negative bacterium / cytosolic large ribosomal subunit / cytoplasmic translation / transcription coactivator activity / tRNA binding / nuclear speck / postsynaptic density / response to xenobiotic stimulus / rRNA binding / ribosome / translation / structural constituent of ribosome / ribonucleoprotein complex / protein domain specific binding / mRNA binding / positive regulation of cell population proliferation / GTPase activity / nucleolus / synapse / GTP binding / negative regulation of transcription by RNA polymerase II / cell surface / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / DNA binding / : / DNA-templated transcription / RNA binding / extracellular exosome / nucleoplasm / zinc ion binding / membrane / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.83 Å | ||||||
Authors | Jomaa, A. / Gamerdinger, M. / Hsieh, H. / Wallisch, A. / Chandrasekaran, V. / Ulusoy, Z. / Scaiola, A. / Hegde, R. / Shan, S. / Ban, N. / Deuerling, E. | ||||||
| Funding support | Switzerland, 1items
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Citation | Journal: Science / Year: 2022Title: 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. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7qwq.cif.gz | 3.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7qwq.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7qwq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qw/7qwq ftp://data.pdbj.org/pub/pdb/validation_reports/qw/7qwq | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 14191MC ![]() 7qwrC ![]() 7qwsC 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 , 4 types, 4 molecules 1578
| #1: RNA chain | Mass: 54095.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
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| #9: RNA chain | Mass: 1539032.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: RNA chain | Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Signal recognition particle ... , 3 types, 3 molecules qvx
| #2: Protein | Mass: 16183.746 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SRP19 / Production host: ![]() |
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| #5: Protein | Mass: 70831.578 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SRP68 / Production host: ![]() |
| #6: Protein | Mass: 55847.734 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: mutant G226E / Source: (gene. exp.) Homo sapiens (human) / Gene: SRP54 / Production host: ![]() References: UniProt: P61011, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
-Protein , 12 types, 12 molecules suABDFmopQXt
| #3: Protein | Mass: 9549.763 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: this will need to changed to UNK / Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
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| #4: Protein | Mass: 17724.037 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BTF3, NACB, OK/SW-cl.8 / Production host: ![]() |
| #7: Protein | Mass: 26570.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 46107.977 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
| #14: Protein | Mass: 34481.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 26662.787 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #31: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: Protein | Mass: 16130.169 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 10299.350 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: Protein | Mass: 21457.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 17768.246 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: Protein | Mass: 23406.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NACA, HSD48 / Production host: ![]() |
+60S ribosomal protein ... , 23 types, 23 molecules bcCEfgGhHiIkLMnOPrRSTZa
-Ribosomal protein ... , 10 types, 10 molecules dejJlNUVWY
| #13: Protein | Mass: 14494.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #15: Protein | Mass: 18350.049 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #26: Protein | Mass: 20288.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #29: Protein | Mass: 6426.759 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #32: Protein | Mass: 24207.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 11836.638 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 14892.505 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #45: Protein | Mass: 17825.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #48: Protein | Mass: 17303.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 102 molecules 


| #53: Chemical | ChemComp-MG / #54: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | N |
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-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
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| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/2 | ||||||||||||||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 95 % |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 2.83 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 51843 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)

Switzerland, 1items
Citation

UCSF Chimera














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