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Yorodumi- PDB-7vqq: Cryo-EM structure of amyloid fibril formed by FUS low complexity ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7vqq | ||||||
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Title | Cryo-EM structure of amyloid fibril formed by FUS low complexity domain | ||||||
Components | fusion protein of mCerulean and FUS LCD | ||||||
Keywords | PROTEIN FIBRIL / amyloid fibril | ||||||
Function / homology | Function and homology information mRNA stabilization / intracellular non-membrane-bounded organelle / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of double-strand break repair via homologous recombination / mRNA Splicing - Major Pathway / RNA splicing / molecular condensate scaffold activity / mRNA 3'-UTR binding / transcription coregulator activity ...mRNA stabilization / intracellular non-membrane-bounded organelle / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of double-strand break repair via homologous recombination / mRNA Splicing - Major Pathway / RNA splicing / molecular condensate scaffold activity / mRNA 3'-UTR binding / transcription coregulator activity / protein homooligomerization / amyloid fibril formation / transcription coactivator activity / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Aequorea victoria (jellyfish) Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.9 Å | ||||||
Authors | Sun, Y.P. / Xia, W.C. / Liu, C. | ||||||
Funding support | 1items
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Citation | Journal: iScience / Year: 2022 Title: Molecular structure of an amyloid fibril formed by FUS low-complexity domain. Authors: Yunpeng Sun / Shenqing Zhang / Jiaojiao Hu / Youqi Tao / Wencheng Xia / Jinge Gu / Yichen Li / Qin Cao / Dan Li / Cong Liu / Abstract: FUS is a multifunctional nuclear protein which undergoes liquid-liquid phase separation in response to stress and DNA damage. Dysregulation of FUS dynamic phase separation leads to formation of ...FUS is a multifunctional nuclear protein which undergoes liquid-liquid phase separation in response to stress and DNA damage. Dysregulation of FUS dynamic phase separation leads to formation of pathological fibril closely associated with neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal dementia. In this study, we determined the cryo-EM structure of a cytotoxic fibril formed by the low-complexity (LC) domain of FUS at 2.9 Å resolution. The fibril structure exhibits a new and extensive serpentine fold consisting of three motifs incorporating together via a Tyr triad. FUS LC employs 91 residues to form an enlarged and stable fibril core via hydrophilic interaction and hydrogen bonds, which is distinct from most of previously determined fibrils commonly stabilized by hydrophobic interaction. Our work reveals the structural basis underlying formation of a cytotoxic and thermostable fibril of FUS LC and sheds light on understanding the liquid-to-solid phase transition of FUS in disease. | ||||||
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 | 7vqq.cif.gz | 71.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7vqq.ent.gz | 43.2 KB | Display | PDB format |
PDBx/mmJSON format | 7vqq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7vqq_validation.pdf.gz | 881.3 KB | Display | wwPDB validaton report |
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Full document | 7vqq_full_validation.pdf.gz | 881.4 KB | Display | |
Data in XML | 7vqq_validation.xml.gz | 18.8 KB | Display | |
Data in CIF | 7vqq_validation.cif.gz | 27 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vq/7vqq ftp://data.pdbj.org/pub/pdb/validation_reports/vq/7vqq | HTTPS FTP |
-Related structure data
Related structure data | 32092MC 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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-Components
#1: Protein | Mass: 51948.352 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: 6His-tagged mCerulean:(FPbase ID: J2JWA, Link: https://www.fpbase.org/protein/mcerulean/) Source: (gene. exp.) Aequorea victoria (jellyfish), (gene. exp.) Homo sapiens (human) Gene: FUS, TLS / Production host: Escherichia coli (E. coli) / References: UniProt: P35637 |
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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 fibril formed by FUS low complexity domain / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: RECOMBINANT | ||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||
Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7.5 | ||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||
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: 40 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
CTF correction | Type: NONE |
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Helical symmerty | Angular rotation/subunit: -1.44 ° / Axial rise/subunit: 5 Å / Axial symmetry: C1 |
3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 171163 / Symmetry type: HELICAL |