[English] 日本語
Yorodumi
- PDB-5yi4: Solution Structure of the DISC1/Ndel1 complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5yi4
TitleSolution Structure of the DISC1/Ndel1 complex
ComponentsDisrupted in schizophrenia 1 homolog,Nuclear distribution protein nudE-like 1
KeywordsPROTEIN BINDING / DISC1 / Ndel1 / coiled coil / psychiatric disorder
Function / homology
Function and homology information


neurofilament cytoskeleton / pyramidal neuron migration to cerebral cortex / cerebral cortex radially oriented cell migration / establishment of chromosome localization / central nervous system neuron axonogenesis / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / radial glia-guided pyramidal neuron migration / mitochondrial calcium ion homeostasis / central region of growth cone / cell proliferation in forebrain ...neurofilament cytoskeleton / pyramidal neuron migration to cerebral cortex / cerebral cortex radially oriented cell migration / establishment of chromosome localization / central nervous system neuron axonogenesis / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / radial glia-guided pyramidal neuron migration / mitochondrial calcium ion homeostasis / central region of growth cone / cell proliferation in forebrain / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / oligopeptidase activity / regulation of dendritic spine development / RHO GTPases Activate Formins / nuclear membrane disassembly / Separation of Sister Chromatids / vesicle transport along microtubule / neurofilament cytoskeleton organization / dynein complex / lysosome localization / axon hillock / microtubule nucleation / regulation of synapse maturation / positive regulation of ubiquitin-dependent protein catabolic process / non-motile cilium assembly / retrograde axonal transport / positive regulation of ruffle assembly / mitotic centrosome separation / protein localization to centrosome / microtubule organizing center / microtubule associated complex / intermediate filament cytoskeleton / inner cell mass cell proliferation / centrosome localization / positive regulation of cell-matrix adhesion / regulation of postsynapse organization / neuron projection extension / ciliary base / kinesin complex / positive regulation of neuroblast proliferation / regulation of intracellular protein transport / positive regulation of axon regeneration / regulation of neuron projection development / cell leading edge / beta-tubulin binding / establishment of mitotic spindle orientation / detection of temperature stimulus involved in sensory perception of pain / kinesin binding / positive regulation of Wnt signaling pathway / cilium assembly / alpha-tubulin binding / TOR signaling / canonical Wnt signaling pathway / positive regulation of axon extension / response to electrical stimulus / GABA-ergic synapse / axon cytoplasm / regulation of synaptic transmission, glutamatergic / ciliary basal body / negative regulation of protein binding / chromosome segregation / neuron migration / kinetochore / positive regulation of neuron projection development / microtubule cytoskeleton organization / spindle / neuron cellular homeostasis / neuron projection development / protein localization / cell migration / synaptic vesicle / insulin receptor signaling pathway / nuclear envelope / nervous system development / cell body / ubiquitin-dependent protein catabolic process / microtubule binding / microtubule / molecular adaptor activity / postsynaptic density / axon / centrosome / glutamatergic synapse / protein-containing complex binding / perinuclear region of cytoplasm / mitochondrion / identical protein binding / cytosol
Similarity search - Function
NUDE domain / Disrupted in schizophrenia 1 / NUDE family / NUDE protein, C-terminal conserved region
Similarity search - Domain/homology
Disrupted in schizophrenia 1 homolog / Nuclear distribution protein nudE-like 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / simulated annealing
AuthorsYe, F. / Yu, C. / Yu, C. / Zhang, M.
Funding support Hong Kong, China, 5items
OrganizationGrant numberCountry
RGC664113 Hong Kong
RGC16103614 Hong Kong
RGCAoE-M09-12 Hong Kong
RGCT13-607/12R Hong Kong
Minister of Science and Technology of China2014CB910204 China
CitationJournal: Neuron / Year: 2017
Title: DISC1 Regulates Neurogenesis via Modulating Kinetochore Attachment of Ndel1/Nde1 during Mitosis.
Authors: Ye, F. / Kang, E. / Yu, C. / Qian, X. / Jacob, F. / Yu, C. / Mao, M. / Poon, R.Y.C. / Kim, J. / Song, H. / Ming, G.L. / Zhang, M.
History
DepositionOct 2, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 15, 2017Provider: repository / Type: Initial release
Revision 1.1May 29, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_nmr_software
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _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.name / _pdbx_nmr_software.name
Revision 1.2Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.3May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Disrupted in schizophrenia 1 homolog,Nuclear distribution protein nudE-like 1


Theoretical massNumber of molelcules
Total (without water)15,4551
Polymers15,4551
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area11450 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

-
Components

#1: Protein Disrupted in schizophrenia 1 homolog,Nuclear distribution protein nudE-like 1 / Protein mNudE-like / mNudE-L


Mass: 15455.417 Da / Num. of mol.: 1 / Fragment: UNP residues 765-852,UNP residues 238-284
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Disc1, Ndel1, Nudel
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q811T9, UniProt: Q9ERR1

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
114anisotropic22D 1H-1H NOESY
121isotropic23D 1H-13C NOESY
132isotropic23D 1H-15N NOESY
143isotropic23D CBCA(CO)NH
153isotropic23D HN(CA)CB

-
Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
solution10.8 mM [U-99% 13C; U-99% 15N] DISC1_Ndel1, 100% D2O13C and 15N sample100% D2O
solution30.8 mM [U-99% 13C; U-99% 15N] DISC1_Ndel1, 90% H2O/10% D2O13C and 15N sample in H2O90% H2O/10% D2O
solution20.8 mM [U-99% 15N] DISC1_Ndel1, 90% H2O/10% D2O15N_sample90% H2O/10% D2O
solid40.8 mM no labelling DISC1_Ndel1, 100% D2Ono labelling100% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.8 mMDISC1_Ndel1[U-99% 13C; U-99% 15N]1
0.8 mMDISC1_Ndel1[U-99% 13C; U-99% 15N]3
0.8 mMDISC1_Ndel1[U-99% 15N]2
0.8 mMDISC1_Ndel1no labelling4
Sample conditionsIonic strength: 50 NaCl mM / Ionic strength err: 0.2 / Label: conditions_1 / pH: 6.5 / Pressure: 1 Pa / Pressure err: 0.01 / Temperature: 303 K / Temperature err: 0.2

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA7501
Varian INOVAVarianINOVA8002

-
Processing

NMR software
NameDeveloperClassification
CNSBrunger A. T. et.al.refinement
CNSBrunger, Adams, Clore, Gros, Nilges and Readstructure calculation
SparkyGoddardchemical shift assignment
SparkyGoddardpeak picking
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more