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Yorodumi- EMDB-70227: amyloid fibril of recombinant full-length 2N4R tau complexed with... -
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Basic information
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| Title | amyloid fibril of recombinant full-length 2N4R tau complexed with mouse liver 18S ribosomal RNA | |||||||||
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Keywords | amyloid fibril / PROTEIN FIBRIL | |||||||||
| 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 / regulation of chromosome organization / intracellular distribution of mitochondria / 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 / main axon / protein polymerization / axolemma / Caspase-mediated cleavage of cytoskeletal proteins / regulation of microtubule polymerization or depolymerization / negative regulation of mitochondrial fission / glial cell projection / neurofibrillary tangle assembly / positive regulation of axon extension / regulation of cellular response to heat / positive regulation of microtubule polymerization / Activation of AMPK downstream of NMDARs / positive regulation of superoxide anion generation / positive regulation of protein localization / cellular response to brain-derived neurotrophic factor stimulus / supramolecular fiber organization / regulation of long-term synaptic depression / cytoplasmic microtubule organization / somatodendritic compartment / regulation of calcium-mediated signaling / synapse assembly / axon cytoplasm / astrocyte activation / phosphatidylinositol binding / nuclear periphery / enzyme inhibitor activity / stress granule assembly / protein phosphatase 2A binding / 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 / regulation of synaptic plasticity / synapse organization / PKR-mediated signaling / SH3 domain binding / response to lead ion / microtubule cytoskeleton organization / memory / cytoplasmic ribonucleoprotein granule / neuron projection development / 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 | helical reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Jiang YX / Sawaya MR / Abskharon R / Ge P / Boyer DR / Eisenberg DS | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: To Be PublishedTitle: RNA contributes to polymorphism of tau amyloid fibrils Authors: Abskharon R / Jiang YX / Ge P / Sawaya MR / Zhang J / Boyer DR / Dolinsky JL / Cascio D / Guo F / Eisenberg DS | |||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_70227.map.gz | 113.9 MB | EMDB map data format | |
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| Header (meta data) | emd-70227-v30.xml emd-70227.xml | 16.7 KB 16.7 KB | Display Display | EMDB header |
| Images | emd_70227.png | 76.4 KB | ||
| Filedesc metadata | emd-70227.cif.gz | 5.8 KB | ||
| Others | emd_70227_half_map_1.map.gz emd_70227_half_map_2.map.gz | 98.4 MB 98.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70227 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70227 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9o8hMC ![]() 9o8eC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_70227.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_70227_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_70227_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : amyloid fibril of recombinant full-length 2N4R tau complexed with...
| Entire | Name: amyloid fibril of recombinant full-length 2N4R tau complexed with mouse liver 18S ribosomal RNA |
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| Components |
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-Supramolecule #1: amyloid fibril of recombinant full-length 2N4R tau complexed with...
| Supramolecule | Name: amyloid fibril of recombinant full-length 2N4R tau complexed with mouse liver 18S ribosomal RNA type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Isoform Tau-F of Microtubule-associated protein tau
| Macromolecule | Name: Isoform Tau-F of Microtubule-associated protein tau / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 46.991012 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQA AAQPHTEIPE GTTAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP P GQKGQANA ...String: MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQA AAQPHTEIPE GTTAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP P GQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AK SRLQTAP VPMPDLKNVK SKIGSTENLK HQPGGGKVQI INKKLDLSNV QSKCGSKDNI KHVPGGGSVQ IVYKPVDLSK VTS KCGSLG NIHHKPGGGQ VEVKSEKLDF KDRVQSKIGS LDNITHVPGG GNKKIETHKL TFRENAKAKT DHGAEIVYKS PVVS GDTSP RHLSNVSSTG SIDMVDSPQL ATLADEVSAS LAKQGLLEHH HHHH UniProtKB: Microtubule-associated protein tau |
-Macromolecule #2: CHLORIDE ION
| Macromolecule | Name: CHLORIDE ION / type: ligand / ID: 2 / Number of copies: 10 / Formula: CL |
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| Molecular weight | Theoretical: 35.453 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.6 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Applied symmetry - Helical parameters - Δz: 2.39525 Å Applied symmetry - Helical parameters - Δ&Phi: 179.634 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 25873 |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| Startup model | Type of model: INSILICO MODEL |
| Final angle assignment | Type: NOT APPLICABLE |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
United States, 2 items
Citation







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FIELD EMISSION GUN
