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Open data
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Basic information
| Entry | Database: PDB / ID: 7rua | ||||||||||||||||||
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| Title | Metazoan pre-targeting GET complex (cBUGG-out) | ||||||||||||||||||
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Keywords | CHAPERONE / ATPase / complex / membrane protein chaperone | ||||||||||||||||||
| Function / homology | Function and homology informationBAT3 complex / immune response-activating cell surface receptor signaling pathway / GET complex / NK T cell activation / ubiquitin-like protein transferase activity / protein carrier activity / : / tail-anchored membrane protein insertion into ER membrane / positive regulation of ERAD pathway / synaptonemal complex assembly ...BAT3 complex / immune response-activating cell surface receptor signaling pathway / GET complex / NK T cell activation / ubiquitin-like protein transferase activity / protein carrier activity / : / tail-anchored membrane protein insertion into ER membrane / positive regulation of ERAD pathway / synaptonemal complex assembly / protein insertion into ER membrane / post-translational protein targeting to endoplasmic reticulum membrane / internal peptidyl-lysine acetylation / misfolded protein binding / endoplasmic reticulum stress-induced pre-emptive quality control / natural killer cell activation / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / ubiquitin-specific protease binding / proteasome binding / regulation of embryonic development / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / polyubiquitin modification-dependent protein binding / negative regulation of proteolysis / ERAD pathway / proteasomal protein catabolic process / synapse assembly / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / lung development / Hsp70 protein binding / molecular function activator activity / protein modification process / kidney development / regulation of protein stability / brain development / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / chromosome / chromatin organization / protein-folding chaperone binding / ribosome binding / spermatogenesis / molecular adaptor activity / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / cell differentiation / protein stabilization / receptor ligand activity / signaling receptor binding / apoptotic process / ubiquitin protein ligase binding / negative regulation of apoptotic process / nucleolus / ATP hydrolysis activity / extracellular exosome / nucleoplasm / ATP binding / membrane / metal ion binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() Homo sapiens (human) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||||||||||||||
Authors | Keszei, A.F.A. / Yip, M.C.J. / Shao, S. | ||||||||||||||||||
| Funding support | United States, 5items
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Citation | Journal: Nat Struct Mol Biol / Year: 2021Title: Structural insights into metazoan pretargeting GET complexes. Authors: Alexander F A Keszei / Matthew C J Yip / Ta-Chien Hsieh / Sichen Shao / ![]() Abstract: Close coordination between chaperones is essential for protein biosynthesis, including the delivery of tail-anchored (TA) proteins containing a single C-terminal transmembrane domain to the ...Close coordination between chaperones is essential for protein biosynthesis, including the delivery of tail-anchored (TA) proteins containing a single C-terminal transmembrane domain to the endoplasmic reticulum (ER) by the conserved GET pathway. For successful targeting, nascent TA proteins must be promptly chaperoned and loaded onto the cytosolic ATPase Get3 through a transfer reaction involving the chaperone SGTA and bridging factors Get4, Ubl4a and Bag6. Here, we report cryo-electron microscopy structures of metazoan pretargeting GET complexes at 3.3-3.6 Å. The structures reveal that Get3 helix 8 and the Get4 C terminus form a composite lid over the Get3 substrate-binding chamber that is opened by SGTA. Another interaction with Get4 prevents formation of Get3 helix 4, which links the substrate chamber and ATPase domain. Both interactions facilitate TA protein transfer from SGTA to Get3. Our findings show how the pretargeting complex primes Get3 for coordinated client loading and ER targeting. | ||||||||||||||||||
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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 | 7rua.cif.gz | 269.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7rua.ent.gz | 212.6 KB | Display | PDB format |
| PDBx/mmJSON format | 7rua.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ru/7rua ftp://data.pdbj.org/pub/pdb/validation_reports/ru/7rua | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 24701MC ![]() 7ru9C ![]() 7rucC C: citing same article ( M: map data used to model this data |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 4 types, 8 molecules ABCFDGEH
| #1: Protein | Mass: 38574.414 Da / Num. of mol.: 2 / Mutation: D68N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q6IQE5, Hydrolases; Acting on acid anhydrides #2: Protein | Mass: 37054.695 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GET4, C7orf20, CEE, TRC35, CGI-20 / Production host: ![]() #3: Protein | Mass: 14618.276 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BAG6, BAT3, G3 / Production host: ![]() #4: Protein | Mass: 18741.480 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UBL4A, DXS254E, GDX, UBL4 / Production host: ![]() |
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-Non-polymers , 3 types, 5 molecules 




| #5: Chemical | | #6: Chemical | #7: 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
| Component | Name: metazoan pre-targeting GET complex cBUGG-out / Type: COMPLEX / Entity ID: #1-#4 / Source: MULTIPLE SOURCES | ||||||||||||
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| Molecular weight | Experimental value: YES | ||||||||||||
| Source (natural) |
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| Source (recombinant) | Organism: ![]() | ||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||
| Vitrification | Cryogen name: ETHANE |
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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 |
| Image recording | Electron dose: 54 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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| Symmetry | Point symmetry: C2 (2 fold cyclic) |
| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35535 / Symmetry type: POINT |
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Homo sapiens (human)
United States, 5items
Citation
UCSF Chimera














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