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Yorodumi- PDB-8d9w: beta-Arf1 homodimeric interface within AP-1, Arf1, Nef, MHC-I lat... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8d9w | ||||||||||||
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| Title | beta-Arf1 homodimeric interface within AP-1, Arf1, Nef, MHC-I lattice on narrow tubes | ||||||||||||
Components |
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Keywords | Protein Transport/Viral Protein / complex / coat / Protein Transport-Viral Protein complex | ||||||||||||
| Function / homology | Function and homology informationbasolateral protein secretion / endosome to melanosome transport / Lysosome Vesicle Biogenesis / AP-1 adaptor complex / mitotic cleavage furrow ingression / trans-Golgi Network Vesicle Budding / protein trimerization / platelet dense granule organization / negative regulation of glycoprotein biosynthetic process / Glycosphingolipid transport ...basolateral protein secretion / endosome to melanosome transport / Lysosome Vesicle Biogenesis / AP-1 adaptor complex / mitotic cleavage furrow ingression / trans-Golgi Network Vesicle Budding / protein trimerization / platelet dense granule organization / negative regulation of glycoprotein biosynthetic process / Glycosphingolipid transport / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / melanosome assembly / regulation of receptor internalization / Intra-Golgi traffic / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / regulation of Arp2/3 complex-mediated actin nucleation / Golgi Associated Vesicle Biogenesis / Synthesis of PIPs at the Golgi membrane / symbiont-mediated suppression of host autophagy / clathrin adaptor activity / symbiont-mediated suppression of host apoptosis / MHC class II antigen presentation / thioesterase binding / Nef Mediated CD4 Down-regulation / CD4 receptor binding / dendritic spine organization / long-term synaptic depression / determination of left/right symmetry / clathrin-coated vesicle / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / TAP complex binding / COPI-dependent Golgi-to-ER retrograde traffic / Golgi medial cisterna / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / clathrin binding / Lysosome Vesicle Biogenesis / Golgi Associated Vesicle Biogenesis / CD8 receptor binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / beta-2-microglobulin binding / Synthesis of PIPs at the plasma membrane / cell leading edge / endoplasmic reticulum exit site / MHC class I protein binding / TAP binding / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / protection from natural killer cell mediated cytotoxicity / host cell Golgi membrane / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / intracellular copper ion homeostasis / detection of bacterium / protein targeting / T cell receptor binding / COPI-mediated anterograde transport / vesicle-mediated transport / viral life cycle / clathrin-coated pit / regulation of calcium-mediated signaling / Neutrophil degranulation / MHC class II antigen presentation / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cytoplasmic vesicle membrane / Nef mediated downregulation of MHC class I complex cell surface expression / sarcomere / trans-Golgi network membrane / small monomeric GTPase / Endosomal/Vacuolar pathway / lumenal side of endoplasmic reticulum membrane / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / intracellular protein transport / kidney development / trans-Golgi network / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / MHC class I peptide loading complex / T cell mediated cytotoxicity / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / MHC class I protein complex / cellular response to virus / peptide antigen binding / SH3 domain binding / positive regulation of T cell mediated cytotoxicity / virion component / positive regulation of type II interferon production / phagocytic vesicle membrane / recycling endosome membrane / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon alpha/beta signaling / synaptic vesicle / antibacterial humoral response / T cell receptor signaling pathway / presynapse / E3 ubiquitin ligases ubiquitinate target proteins / heart development Similarity search - Function | ||||||||||||
| Biological species | ![]() Human immunodeficiency virus 1 Homo sapiens (human)![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 9.3 Å | ||||||||||||
Authors | Hooy, R.H. / Hurley, J.H. | ||||||||||||
| Funding support | United States, 3items
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Citation | Journal: Sci Adv / Year: 2022Title: Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat. Authors: Richard M Hooy / Yuichiro Iwamoto / Dan A Tudorica / Xuefeng Ren / James H Hurley / ![]() Abstract: The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to ...The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to sequester major histocompatibility complex class I (MHC-I), evading immune detection. We found that AP-1:Arf1:Nef:MHC-I forms a coat on tubulated membranes without clathrin and determined its structure. The coat assembles via Arf1 dimer interfaces. AP-1-positive tubules are enriched in cells upon clathrin knockdown. Nef localizes preferentially to AP-1 tubules in cells, explaining how Nef sequesters MHC-I. Coat contact residues are conserved across Arf isoforms and the Arf-dependent AP complexes AP-1, AP-3, and AP-4. Thus, AP complexes can self-assemble with Arf1 into tubular coats without clathrin or other scaffolding factors. The AP-1:Arf1 coat defines the structural basis of a broader class of tubulovesicular membrane coats as an intermediate in clathrin vesicle formation from internal membranes and as an MHC-I sequestration mechanism in HIV-1 infection. | ||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8d9w.cif.gz | 582.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8d9w.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8d9w.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8d9w_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 8d9w_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 8d9w_validation.xml.gz | 70.3 KB | Display | |
| Data in CIF | 8d9w_validation.cif.gz | 120.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d9/8d9w ftp://data.pdbj.org/pub/pdb/validation_reports/d9/8d9w | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 27186MC ![]() 7ux3C ![]() 8d4cC ![]() 8d4dC ![]() 8d4eC ![]() 8d4fC ![]() 8d4gC ![]() 8d9rC ![]() 8d9sC ![]() 8d9tC ![]() 8d9uC ![]() 8d9vC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 2 types, 6 molecules NUVdFI
| #1: Protein | Mass: 24285.244 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Glycine 2 is myristoylated / Source: (gene. exp.) ![]() Human immunodeficiency virus 1 / Gene: nef / Production host: ![]() #5: Protein | Mass: 20590.547 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Gly2 is myristoylated / Source: (gene. exp.) Homo sapiens (human) / Gene: ARF1 / Production host: ![]() |
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-Protein/peptide , 1 types, 2 molecules Yj
| #2: Protein/peptide | Mass: 4542.884 Da / Num. of mol.: 2 / Mutation: T345S, S349G, G355S, C363A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Production host: ![]() |
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-AP-1 complex subunit ... , 4 types, 12 molecules BADEMXZaKOef
| #3: Protein | Mass: 104736.461 Da / Num. of mol.: 4 / Mutation: K359R,E476K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AP1B1, ADTB1, BAM22, CLAPB2 / Production host: ![]() #4: Protein | Mass: 48606.730 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #6: Protein | Mass: 68194.094 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #7: Protein | Mass: 18305.273 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AP1S3 / Production host: ![]() |
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-Non-polymers , 2 types, 4 molecules 


| #8: Chemical | | #9: Chemical | |
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-Details
| Has ligand of interest | Y |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: subtomogram averaging |
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Sample preparation
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| Buffer solution | pH: 7.2 | ||||||||||||||||||
| Specimen | Conc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 42000 X / Nominal defocus max: 4500 nm / Nominal defocus min: 1500 nm / Alignment procedure: COMA FREE |
| Image recording | Electron dose: 2.7 e/Å2 / Avg electron dose per subtomogram: 120 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
| EM imaging optics | Energyfilter slit width: 25 eV |
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Processing
| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
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| Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 9.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8174 / Symmetry type: POINT | ||||||||||||||||||||||||
| EM volume selection | Num. of tomograms: 38 / Num. of volumes extracted: 43110 | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 31 Å2 | ||||||||||||||||||||||||
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About Yorodumi




Human immunodeficiency virus 1
Homo sapiens (human)

United States, 3items
Citation






















PDBj

































FIELD EMISSION GUN