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- PDB-9rux: Cryo-EM structure of DISC1 core -

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Basic information

Entry
Database: PDB / ID: 9rux
TitleCryo-EM structure of DISC1 core
ComponentsDisrupted in schizophrenia 1 homolog
KeywordsSTRUCTURAL PROTEIN / Scaffold / complex / tetramer / coiled coil / UVR domain / psychiatric disorder
Function / homology
Function and homology information


pyramidal neuron migration to cerebral cortex / mitochondrial calcium ion homeostasis / cell proliferation in forebrain / central region of growth cone / cerebral cortex radially oriented cell migration / regulation of dendritic spine development / dynein complex / regulation of synapse maturation / intermediate filament cytoskeleton / non-motile cilium assembly ...pyramidal neuron migration to cerebral cortex / mitochondrial calcium ion homeostasis / cell proliferation in forebrain / central region of growth cone / cerebral cortex radially oriented cell migration / regulation of dendritic spine development / dynein complex / regulation of synapse maturation / intermediate filament cytoskeleton / non-motile cilium assembly / protein localization to centrosome / regulation of postsynapse organization / positive regulation of ubiquitin-dependent protein catabolic process / kinesin complex / positive regulation of cell-matrix adhesion / positive regulation of neuroblast proliferation / ciliary base / regulation of neuron projection development / detection of temperature stimulus involved in sensory perception of pain / microtubule organizing center / TOR signaling / cilium assembly / response to electrical stimulus / canonical Wnt signaling pathway / kinesin binding / positive regulation of Wnt signaling pathway / positive regulation of axon extension / regulation of synaptic transmission, glutamatergic / positive regulation of neuron projection development / GABA-ergic synapse / microtubule cytoskeleton organization / neuron migration / synaptic vesicle / intracellular protein localization / nervous system development / presynapse / cell body / molecular adaptor activity / microtubule / postsynaptic density / ciliary basal body / axon / centrosome / protein-containing complex binding / perinuclear region of cytoplasm / glutamatergic synapse / mitochondrion / identical protein binding / cytosol
Similarity search - Function
Disrupted in schizophrenia 1
Similarity search - Domain/homology
Disrupted in schizophrenia 1 homolog
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsZhou, J.C.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome Trust United Kingdom
CitationJournal: Nat Commun / Year: 2026
Title: The schizophrenia associated protein DISC1 forms a multivalent tetrameric hub via conserved UVR dimers.
Authors: Jin Chuan Zhou / Jiri Kratochvil / Fei Ye / Kamel El Omari / Philipp Kukura / Mingjie Zhang / Elena Seiradake /
Abstract: DISC1 is a pleiotropic protein with essential roles in neuronal proliferation and migration, intracellular signalling and cargo transport. It associates with a diverse array of partner molecules in ...DISC1 is a pleiotropic protein with essential roles in neuronal proliferation and migration, intracellular signalling and cargo transport. It associates with a diverse array of partner molecules in these contexts. Mutations at the DISC1 locus are strongly associated with a spectrum of mental illnesses such as schizophrenia and depression. Despite its clinical relevance, the molecular architecture and function of DISC1 have remained largely elusive. We present a cryo-EM structure of the entire conserved core region of DISC1. The structure reveals an intricate homotetrameric assembly that harbours conserved bacteria-derived UVR domains. Four of these domains, one from each monomer, mediate extensive contacts forming two asymmetric dimer units. The dimers in turn interface with each other at two distinct coiled coil domains to achieve a two-fold symmetric tetramer. Mutational analysis shows that this tetrameric architecture enables DISC1 to simultaneously bind multiple copies of NDE1 client protein. Importantly, tetramerization and partner binding are structurally independent functions of DISC1. Altogether, our study provides a compelling molecular model of an ancient bacteria protein fold participating in the assembly of a multivalent mammalian scaffold hub that can coordinate multiple partner molecules.
History
DepositionJul 5, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 6, 2026Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0May 6, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Disrupted in schizophrenia 1 homolog
B: Disrupted in schizophrenia 1 homolog
C: Disrupted in schizophrenia 1 homolog
D: Disrupted in schizophrenia 1 homolog


Theoretical massNumber of molelcules
Total (without water)215,3604
Polymers215,3604
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable, light scattering, SEC-MALS
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Disrupted in schizophrenia 1 homolog


Mass: 53839.914 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Disc1 / Plasmid: pET32 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q811T9
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Tetrameric complex of mDISC1 core / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.17 MDa / Experimental value: YES
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: BL21 / Plasmid: pET32
Buffer solutionpH: 8
Buffer component
IDConc.NameFormulaBuffer-ID
150 mMTrisC4H11NO31
2300 mMsodium chlorideNaCl1
35 mMDTTC4H10O2S21
40.4 %CHAPSC32H58N2O7S1
SpecimenConc.: 2.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Monodisperse
Specimen supportDetails: 15mA / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 294 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 1750 nm / Nominal defocus min: 1250 nm / Cs: 2.7 mm / Alignment procedure: BASIC
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 6039
EM imaging opticsEnergyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
4cryoSPARCCTF correction
7UCSF ChimeraXmodel fitting
8ISOLDEmodel fitting
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
12cryoSPARCclassification
13cryoSPARC3D reconstruction
14PHENIX1.20.1_4487:model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1439840
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 227140 / Num. of class averages: 2 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT
Atomic model buildingAccession code: AF-Q811T9-F1-v4 / Chain residue range: 322-722 / Source name: AlphaFold / Type: in silico model
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0049712
ELECTRON MICROSCOPYf_angle_d0.54113084
ELECTRON MICROSCOPYf_dihedral_angle_d11.3873776
ELECTRON MICROSCOPYf_chiral_restr0.0311516
ELECTRON MICROSCOPYf_plane_restr0.0051688

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