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Open data
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Basic information
| Entry | Database: PDB / ID: 9ofw | |||||||||||||||||||||||||||
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| Title | 328-363 tau mutant S341L_S352I | |||||||||||||||||||||||||||
Components | Microtubule-associated protein tau | |||||||||||||||||||||||||||
Keywords | PROTEIN FIBRIL / tau / aggregation | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationplus-end-directed organelle transport along microtubule / histone-dependent DNA binding / negative regulation of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / axonal transport / tubulin complex / positive regulation of protein localization to synapse / phosphatidylinositol bisphosphate binding / generation of neurons ...plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / negative regulation of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / axonal transport / tubulin complex / positive regulation of protein localization to synapse / phosphatidylinositol bisphosphate binding / generation of neurons / rRNA metabolic process / axonal transport of mitochondrion / regulation of mitochondrial fission / axon development / regulation of microtubule-based movement / intracellular distribution of mitochondria / regulation of chromosome organization / central nervous system neuron development / minor groove of adenine-thymine-rich DNA binding / lipoprotein particle binding / microtubule polymerization / negative regulation of mitochondrial membrane potential / regulation of microtubule polymerization / dynactin binding / apolipoprotein binding / protein polymerization / main axon / Caspase-mediated cleavage of cytoskeletal proteins / regulation of microtubule polymerization or depolymerization / negative regulation of mitochondrial fission / axolemma / glial cell projection / neurofibrillary tangle assembly / positive regulation of axon extension / positive regulation of microtubule polymerization / regulation of cellular response to heat / Activation of AMPK downstream of NMDARs / positive regulation of protein localization / positive regulation of superoxide anion generation / supramolecular fiber organization / cellular response to brain-derived neurotrophic factor stimulus / regulation of long-term synaptic depression / cytoplasmic microtubule organization / regulation of calcium-mediated signaling / somatodendritic compartment / axon cytoplasm / synapse assembly / phosphatidylinositol binding / nuclear periphery / astrocyte activation / enzyme inhibitor activity / protein phosphatase 2A binding / stress granule assembly / regulation of microtubule cytoskeleton organization / regulation of autophagy / cellular response to reactive oxygen species / microglial cell activation / cellular response to nerve growth factor stimulus / Hsp90 protein binding / protein homooligomerization / SH3 domain binding / PKR-mediated signaling / regulation of synaptic plasticity / synapse organization / response to lead ion / microtubule cytoskeleton organization / memory / neuron projection development / cytoplasmic ribonucleoprotein granule / cell-cell signaling / single-stranded DNA binding / cellular response to heat / protein-folding chaperone binding / growth cone / microtubule cytoskeleton / actin binding / cell body / double-stranded DNA binding / microtubule binding / sequence-specific DNA binding / amyloid fibril formation / dendritic spine / microtubule / protein-macromolecule adaptor activity / learning or memory / neuron projection / membrane raft / negative regulation of gene expression / axon / neuronal cell body / DNA damage response / dendrite / protein kinase binding / enzyme binding / mitochondrion / DNA binding / RNA binding / extracellular region / identical protein binding / nucleus Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||||||||||||||||||||
Authors | Dashnaw, C.M. / Joachimiak, L. | |||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: 328-363 tau mutant S341L_S352I Authors: Dashnaw, C.M. / Joachimiak, L. | |||||||||||||||||||||||||||
| History |
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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 | 9ofw.cif.gz | 64.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ofw.ent.gz | 50.7 KB | Display | PDB format |
| PDBx/mmJSON format | 9ofw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/of/9ofw ftp://data.pdbj.org/pub/pdb/validation_reports/of/9ofw | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 70445MC 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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Components
| #1: Protein/peptide | Mass: 1695.981 Da / Num. of mol.: 20 / Mutation: S352I / Source method: obtained synthetically Details: This sequence is a chemically synthesized S341L, S352I mutant variant of human tau 328-363 truncation. Source: (synth.) Homo sapiens (human) / References: UniProt: P10636Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
| Component | Name: 328-363 tau construct with S341L and S352I mutations / Type: COMPLEX Details: Fibrils generated by aggregation in 10 mM NaPO4, 200 mM MgCl2. Peptide was chemically synthesized. Entity ID: all / Source: RECOMBINANT | |||||||||||||||
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| Molecular weight | Experimental value: NO | |||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||
| Source (recombinant) | Organism: Homo sapiens (human) | |||||||||||||||
| Buffer solution | pH: 7.4 / Details: 10mM NaPO4, 200mM MgCl2, pH 7.4 | |||||||||||||||
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| Specimen | Conc.: 4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: 328-363 tau peptide with S341L and S352I mutations was chemically synthesized. Peptide was aggregated in 10 mM NaPO4, 200 mM MgCl2. | |||||||||||||||
| Specimen support | Details: The grid was glow discharged prior to use. / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 279 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 defocus max: 2200 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||
| Helical symmerty | Angular rotation/subunit: -1.29 ° / Axial rise/subunit: 4.75 Å / Axial symmetry: C1 | ||||||||||||||||
| 3D reconstruction | Resolution: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 152763 / Symmetry type: HELICAL | ||||||||||||||||
| Atomic model building | B value: 32.57 / Protocol: AB INITIO MODEL | ||||||||||||||||
| Atomic model building | Details: Cryfold / Source name: Other / Type: in silico model |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation
PDBj






FIELD EMISSION GUN