[English] 日本語
Yorodumi
- PDB-1gt0: Crystal structure of a POU/HMG/DNA ternary complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1gt0
TitleCrystal structure of a POU/HMG/DNA ternary complex
Components
  • 5'-D(*AP*TP*CP*CP*CP*AP*TP*TP*AP*GP* CP*AP*TP*CP*CP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3'
  • 5'-D(*TP*TP*CP*TP*TP*TP*GP*TP*TP*TP* GP*GP*AP* TP*GP*CP*TP*AP*AP*TP*GP*GP*GP*A)-3'
  • OCTAMER-BINDING TRANSCRIPTION FACTOR 1
  • TRANSCRIPTION FACTOR SOX-2
KeywordsTRANSCRIPTION / TRANSCRIPTION FACTOR / POU FACTORS / SOX PROTEINS
Function / homology
Function and homology information


diencephalon morphogenesis / olfactory placode formation / lens induction in camera-type eye / retina morphogenesis in camera-type eye / regulation of myofibroblast cell apoptotic process / detection of mechanical stimulus involved in equilibrioception / pigment biosynthetic process / forebrain neuron differentiation / anatomical structure formation involved in morphogenesis / adenohypophysis development ...diencephalon morphogenesis / olfactory placode formation / lens induction in camera-type eye / retina morphogenesis in camera-type eye / regulation of myofibroblast cell apoptotic process / detection of mechanical stimulus involved in equilibrioception / pigment biosynthetic process / forebrain neuron differentiation / anatomical structure formation involved in morphogenesis / adenohypophysis development / response to oxygen-glucose deprivation / positive regulation of epithelial cell differentiation / endodermal cell fate specification / Deactivation of the beta-catenin transactivating complex / negative regulation of cell cycle G1/S phase transition / positive regulation of cell-cell adhesion / detection of mechanical stimulus involved in sensory perception of sound / neuron fate commitment / trophectodermal cell differentiation / neuronal stem cell population maintenance / male genitalia development / RNA Polymerase III Transcription Initiation From Type 3 Promoter / response to growth factor / RNA Polymerase III Abortive And Retractive Initiation / miRNA binding / cell fate specification / tongue development / inner ear morphogenesis / epithelial tube branching involved in lung morphogenesis / positive regulation of neuroblast proliferation / negative regulation of Wnt signaling pathway / stem cell population maintenance / lung alveolus development / positive regulation of Notch signaling pathway / somatic stem cell population maintenance / negative regulation of cell differentiation / RNA polymerase II transcribes snRNA genes / neuroblast proliferation / negative regulation of neuron differentiation / regulation of neurogenesis / anatomical structure morphogenesis / negative regulation of osteoblast differentiation / RNA polymerase II core promoter sequence-specific DNA binding / embryonic organ development / cell fate commitment / response to retinoic acid / Notch signaling pathway / cellular response to cadmium ion / positive regulation of neuron differentiation / response to organic substance / stem cell differentiation / positive regulation of cell differentiation / sensory perception of sound / negative regulation of canonical Wnt signaling pathway / cerebral cortex development / chromatin DNA binding / neuron differentiation / osteoblast differentiation / Wnt signaling pathway / positive regulation of miRNA transcription / RNA polymerase II transcription regulator complex / negative regulation of epithelial cell proliferation / gene expression / regulation of gene expression / DNA-binding transcription activator activity, RNA polymerase II-specific / Interleukin-4 and Interleukin-13 signaling / DNA-binding transcription factor binding / Estrogen-dependent gene expression / transcription regulator complex / RNA polymerase II-specific DNA-binding transcription factor binding / sequence-specific DNA binding / positive regulation of MAPK cascade / cell differentiation / transcription cis-regulatory region binding / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / chromatin binding / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
POU domain, class 2, transcription factor 1, C-terminal / POU domain, class 2, transcription factor 1 C-terminal / Octamer-binding transcription factor / Transcription factor SOX / SOX transcription factor / POU-specific domain / POU domain / Pou domain - N-terminal to homeobox domain / POU-specific (POUs) domain signature 1. / POU-specific (POUs) domain signature 2. ...POU domain, class 2, transcription factor 1, C-terminal / POU domain, class 2, transcription factor 1 C-terminal / Octamer-binding transcription factor / Transcription factor SOX / SOX transcription factor / POU-specific domain / POU domain / Pou domain - N-terminal to homeobox domain / POU-specific (POUs) domain signature 1. / POU-specific (POUs) domain signature 2. / POU-specific (POUs) domain profile. / Found in Pit-Oct-Unc transcription factors / High mobility group box domain / DNA Binding (I), subunit A / Homeobox, conserved site / 'Homeobox' domain signature. / Homeodomain / 'Homeobox' domain profile. / Homeodomain / lambda repressor-like DNA-binding domains / Homeobox domain / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / 434 Repressor (Amino-terminal Domain) / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Lambda repressor-like, DNA-binding domain superfamily / Homeodomain-like / Homeobox-like domain superfamily / Arc Repressor Mutant, subunit A / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
DNA / DNA (> 10) / POU domain, class 2, transcription factor 1 / Transcription factor SOX-2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MUS MUSCULUS (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å
AuthorsRemenyi, A. / Wilmanns, M.
CitationJournal: Genes Dev. / Year: 2003
Title: Crystal Structure of a POU/Hmg/DNA Ternary Complex Suggests Differential Assembly of Oct4 and Sox2 on Two Enhancers
Authors: Remenyi, A. / Lins, K. / Nissen, L.J. / Reinbold, R. / Scholer, H.R. / Wilmanns, M.
History
DepositionJan 9, 2002Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 30, 2003Provider: repository / Type: Initial release
Revision 1.1Nov 14, 2012Group: Database references / Derived calculations ...Database references / Derived calculations / Non-polymer description / Other / Refinement description
Revision 1.2Jul 24, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 5'-D(*TP*TP*CP*TP*TP*TP*GP*TP*TP*TP* GP*GP*AP* TP*GP*CP*TP*AP*AP*TP*GP*GP*GP*A)-3'
B: 5'-D(*AP*TP*CP*CP*CP*AP*TP*TP*AP*GP* CP*AP*TP*CP*CP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3'
C: OCTAMER-BINDING TRANSCRIPTION FACTOR 1
D: TRANSCRIPTION FACTOR SOX-2


Theoretical massNumber of molelcules
Total (without water)42,8984
Polymers42,8984
Non-polymers00
Water1,62190
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)72.800, 72.800, 172.400
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

-
Components

#1: DNA chain 5'-D(*TP*TP*CP*TP*TP*TP*GP*TP*TP*TP* GP*GP*AP* TP*GP*CP*TP*AP*AP*TP*GP*GP*GP*A)-3'


Mass: 7436.796 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: FGF-4 ENHANCER / Source: (synth.) MUS MUSCULUS (house mouse)
#2: DNA chain 5'-D(*AP*TP*CP*CP*CP*AP*TP*TP*AP*GP* CP*AP*TP*CP*CP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3'


Mass: 7299.773 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: FGF-4 ENHANCER / Source: (synth.) MUS MUSCULUS (house mouse)
#3: Protein OCTAMER-BINDING TRANSCRIPTION FACTOR 1 / OTF-1 / NF-A1 / OCT-1


Mass: 18327.795 Da / Num. of mol.: 1 / Fragment: POU DOMAIN RESIDUES 280-438 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET-24D / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P14859
#4: Protein TRANSCRIPTION FACTOR SOX-2


Mass: 9833.532 Da / Num. of mol.: 1 / Fragment: HMG DOMAIN RESIDUES 41-120
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PET24-D / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P48432
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 90 / Source method: isolated from a natural source / Formula: H2O
Compound detailsCHAIN C ENGINEERED MUTATION CYS340SER CYS428SER

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.1 Å3/Da / Density % sol: 60 %
Crystal growpH: 7
Details: 18% PEG3350, 50 MM HEPES PH 7.0, 20 MM MGCL2, 5% GLYCEROL

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.846
DetectorType: MARRESEARCH / Detector: CCD / Date: Jun 15, 2001
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.846 Å / Relative weight: 1
ReflectionResolution: 2.6→30 Å / Num. obs: 16619 / % possible obs: 98.3 % / Redundancy: 5.2 % / Biso Wilson estimate: 80.3 Å2 / Rmerge(I) obs: 0.047 / Rsym value: 0.047 / Net I/σ(I): 21.8
Reflection shellResolution: 2.6→2.69 Å / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2.5 / Rsym value: 0.35 / % possible all: 96.5

-
Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
SHELXphasing
SHARPphasing
CNS1refinement
RefinementMethod to determine structure: MAD / Resolution: 2.6→30 Å / Data cutoff high absF: 100000 / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.285 836 5 %RANDOM
Rwork0.232 ---
obs0.232 16612 98.2 %-
Displacement parametersBiso mean: 58.3 Å2
Refinement stepCycle: LAST / Resolution: 2.6→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1765 978 0 90 2833
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.01
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.8
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
LS refinement shellResolution: 2.6→2.66 Å / Rfactor Rfree error: 0.061 / Total num. of bins used: 16
RfactorNum. reflection% reflection
Rfree0.4005 42 5 %
Rwork0.3935 858 -
obs--5.4 %

+
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