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- PDB-6a6b: cryo-em structure of alpha-synuclein fiber -

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Database: PDB / ID: 6a6b
Titlecryo-em structure of alpha-synuclein fiber
KeywordsPROTEIN FIBRIL / alpha-syn fiber / Parkinson disease
Function / homologyAmyloid fiber formation / Synuclein / Synuclein / Alpha-synuclein / regulation of phospholipase activity / regulation of acyl-CoA biosynthetic process / neutral lipid metabolic process / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of mitochondrial electron transport, NADH to ubiquinone / response to desipramine ...Amyloid fiber formation / Synuclein / Synuclein / Alpha-synuclein / regulation of phospholipase activity / regulation of acyl-CoA biosynthetic process / neutral lipid metabolic process / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of mitochondrial electron transport, NADH to ubiquinone / response to desipramine / negative regulation of monooxygenase activity / negative regulation of norepinephrine uptake / positive regulation of glutathione peroxidase activity / positive regulation of hydrogen peroxide catabolic process / supramolecular fiber / mitochondrial membrane organization / regulation of glutamate secretion / regulation of reactive oxygen species biosynthetic process / negative regulation of transporter activity / negative regulation of chaperone-mediated autophagy / regulation of locomotion / regulation of norepinephrine uptake / regulation of synaptic vesicle recycling / negative regulation of platelet-derived growth factor receptor signaling pathway / negative regulation of exocytosis / positive regulation of inositol phosphate biosynthetic process / response to iron(II) ion / positive regulation of neurotransmitter secretion / negative regulation of serotonin uptake / mitochondrial ATP synthesis coupled electron transport / dopamine biosynthetic process / negative regulation of histone acetylation / synaptic vesicle transport / negative regulation of microtubule polymerization / dopamine uptake involved in synaptic transmission / nuclear outer membrane / positive regulation of receptor recycling / regulation of dopamine secretion / regulation of macrophage activation / dynein complex binding / negative regulation of dopamine metabolic process / positive regulation of endocytosis / beta-tubulin binding / supramolecular fiber organization / alpha-tubulin binding / phospholipase binding / kinesin binding / response to magnesium ion / response to interferon-gamma / negative regulation of thrombin-activated receptor signaling pathway / cuprous ion binding / cellular response to fibroblast growth factor stimulus / synaptic vesicle endocytosis / regulation of presynapse assembly / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / behavioral response to cocaine / response to interleukin-1 / excitatory postsynaptic potential / inclusion body / regulation of transmembrane transporter activity / Hsp70 protein binding / microglial cell activation / synapse organization / adult locomotory behavior / cellular response to epinephrine stimulus / phospholipid metabolic process / positive regulation of protein serine/threonine kinase activity / long-term synaptic potentiation / fatty acid metabolic process / rough endoplasmic reticulum / negative regulation of protein phosphorylation / receptor internalization / ferrous iron binding / positive regulation of release of sequestered calcium ion into cytosol / synaptic vesicle membrane / cellular response to copper ion / protein destabilization / negative regulation of neuron death / regulation of long-term neuronal synaptic plasticity / phosphoprotein binding / tau protein binding / terminal bouton / positive regulation of inflammatory response / phospholipid binding / mitochondrial intermembrane space / postsynapse / actin cytoskeleton / activation of cysteine-type endopeptidase activity involved in apoptotic process / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of neuron death / cell cortex / cellular response to oxidative stress / growth cone / actin binding / mitochondrial inner membrane / histone binding / transcription regulatory region DNA binding / positive regulation of peptidyl-serine phosphorylation / protein N-terminus binding / ribosome
Function and homology information
Specimen sourceHomo sapiens (human)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / 3.07 Å resolution
AuthorsLi, Y.W. / Zhao, C.Y. / Luo, F. / Liu, Z. / Gui, X. / Luo, Z. / Zhang, X. / Li, D. / Liu, C. / Li, X.
CitationJournal: Cell Res. / Year: 2018
Title: Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy.
Authors: Yaowang Li / Chunyu Zhao / Feng Luo / Zhenying Liu / Xinrui Gui / Zhipu Luo / Xiang Zhang / Dan Li / Cong Liu / Xueming Li
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Jun 27, 2018 / Release: Jul 11, 2018
RevisionDateData content typeGroupCategoryItemProviderType
1.0Jul 11, 2018Structure modelrepositoryInitial release
1.1Aug 1, 2018Structure modelData collection / Derived calculationspdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop
1.2Oct 24, 2018Structure modelData collection / Database referencescitation / citation_author_citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name

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Deposited unit
A: Alpha-synuclein
B: Alpha-synuclein
C: Alpha-synuclein
D: Alpha-synuclein
E: Alpha-synuclein
F: Alpha-synuclein
G: Alpha-synuclein
H: Alpha-synuclein
I: Alpha-synuclein
J: Alpha-synuclein
K: Alpha-synuclein
L: Alpha-synuclein

Theoretical massNumber of molelcules
Total (without water)75,01312

  • idetical with deposited unit
  • defined by author
  • Evidence: microscopy, TEM, AFM and x-ray diffraction
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TypeNameSymmetry operationNumber
identity operation1_5551
Buried area (Å2)50960
ΔGint (kcal/M)-185
Surface area (Å2)26990


#1: Protein/peptide
Alpha-synuclein / / Non-A beta component of AD amyloid / Non-A4 component of amyloid precursor / NACP

Mass: 6251.097 Da / Num. of mol.: 12 / Fragment: UNP residues 37-99 / Source: (gene. exp.) Homo sapiens (human) / Gene: SNCA, NACP, PARK1 / Production host: Escherichia coli K-12 (bacteria) / References: UniProt: P37840

Experimental details


EM experimentAggregation state: FILAMENT / Reconstruction method: helical reconstruction

Sample preparation

ComponentName: alpha-synuclein fiber / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli K-12 (bacteria)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: 4 microl of alpha-syn fibril solution was applied to a glow-discharged holey carbon grid (Quantifoil R1.2/1.3, 300 mesh), blotted for 6 s, and plunge-frozen in liquid ethane using FEI Vitrobot Mark IV. 95% humidity, 16 degrees
Grid material: COPPER / Grid mesh size: 300 / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 289

Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingAverage exposure time: 8 / Electron dose: 50 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)
Image scansMovie frames/image: 32 / Used frames/image: 1-32


EM software
4CTFFIND4CTF correction
13RELION2.13D reconstruction
Helical symmertyAngular rotation/subunit: 179.641 / Axial rise/subunit: 2.393 / Axial symmetry: C1
3D reconstructionResolution: 3.07 / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 43677 / Symmetry type: HELICAL

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