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Yorodumi- PDB-6vps: Cryo-EM structure of the amyloid core of Drosophila Orb2 isolated... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6vps | ||||||
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Title | Cryo-EM structure of the amyloid core of Drosophila Orb2 isolated from head | ||||||
Components | Translational regulator orb2 | ||||||
Keywords | PROTEIN FIBRIL / amyloid / prion-like / long-term memory | ||||||
Function / homology | Function and homology information dendrite terminus / : / sperm axoneme assembly / male courtship behavior / asymmetric cell division / sperm individualization / translation activator activity / translation factor activity, RNA binding / male meiosis I / negative regulation of cytoplasmic translation ...dendrite terminus / : / sperm axoneme assembly / male courtship behavior / asymmetric cell division / sperm individualization / translation activator activity / translation factor activity, RNA binding / male meiosis I / negative regulation of cytoplasmic translation / long-term memory / axon terminus / mRNA regulatory element binding translation repressor activity / positive regulation of translation / synaptic membrane / mRNA 3'-UTR binding / ribosome binding / presynapse / cell cortex / cell body / spermatogenesis / perikaryon / postsynapse / negative regulation of translation / protein stabilization / neuron projection / axon / synapse / perinuclear region of cytoplasm / protein-containing complex / RNA binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.6 Å | ||||||
Authors | Hervas, R. / Rau, M.J. / Park, Y. / Zhang, W. / Murzin, A.G. / Fitzpatrick, J.A.J. / Scheres, S.H.W. / Si, K. | ||||||
Citation | Journal: Science / Year: 2020 Title: Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in . Authors: Ruben Hervas / Michael J Rau / Younshim Park / Wenjuan Zhang / Alexey G Murzin / James A J Fitzpatrick / Sjors H W Scheres / Kausik Si / Abstract: How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element-binding (CPEB) protein, is a ...How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element-binding (CPEB) protein, is a putative substrate of long-lasting memories. We isolated aggregated CPEB, Orb2, from adult heads and determined its activity and atomic structure, at 2.6-angstrom resolution, using cryo-electron microscopy. Orb2 formed ~75-nanometer-long threefold-symmetric amyloid filaments. Filament formation transformed Orb2 from a translation repressor to an activator and "seed" for further translationally active aggregation. The 31-amino acid protofilament core adopted a cross-β unit with a single hydrophilic hairpin stabilized through interdigitated glutamine packing. Unlike the hydrophobic core of pathogenic amyloids, the hydrophilic core of Orb2 filaments suggests how some neuronal amyloids could be a stable yet regulatable substrate of memory. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6vps.cif.gz | 72.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6vps.ent.gz | 56.9 KB | Display | PDB format |
PDBx/mmJSON format | 6vps.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6vps_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 6vps_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6vps_validation.xml.gz | 22.6 KB | Display | |
Data in CIF | 6vps_validation.cif.gz | 33.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vp/6vps ftp://data.pdbj.org/pub/pdb/validation_reports/vp/6vps | HTTPS FTP |
-Related structure data
Related structure data | 21316MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Symmetry | Helical symmetry: (Circular symmetry: 3 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 9 / Rise per n subunits: 4.75 Å / Rotation per n subunits: -1.55 °) |
-Components
#1: Protein/peptide | Mass: 3974.170 Da / Num. of mol.: 9 / Fragment: UNP residues 176-206 / Source method: isolated from a natural source / Source: (natural) Drosophila melanogaster (fruit fly) / References: UniProt: Q9VSR3 |
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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 |
-Sample preparation
Component | Name: amyloid core of Drosophila Orb2 / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) / Tissue: head |
Buffer solution | pH: 7.25 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
-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: 63 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
Software | Name: REFMAC / Version: 5.8.0256 / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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CTF correction | Type: NONE | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: -1.55 ° / Axial rise/subunit: 4.75 Å / Axial symmetry: C3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19509 / Symmetry type: HELICAL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | Resolution: 2.6→86.72 Å / Cor.coef. Fo:Fc: 0.854 / WRfactor Rwork: 0.322 / SU B: 10.458 / SU ML: 0.21 / Average fsc overall: 0.8918 / Average fsc work: 0.8918 / ESU R: 0.37 Details: Hydrogens have been added in their riding positions
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Solvent computation | Solvent model: BABINET MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.615 Å2
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Refine LS restraints |
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LS refinement shell | Refine-ID: ELECTRON MICROSCOPY / Num. reflection Rfree: _ / Total num. of bins used: 20 / % reflection obs: 100 %
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