[English] 日本語
Yorodumi
- PDB-4om2: Crystal structure of TLE1 N-terminal Q-domain residues 1-156 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4om2
TitleCrystal structure of TLE1 N-terminal Q-domain residues 1-156
ComponentsTransducin-like enhancer protein 1
KeywordsTranscription / DNA binding / tetramer / helix-turn-helix / Wnt repressor / TCF/LEF
Function / homology
Function and homology information


Repression of WNT target genes / beta-catenin-TCF complex / negative regulation of Wnt signaling pathway / negative regulation of anoikis / negative regulation of canonical NF-kappaB signal transduction / Deactivation of the beta-catenin transactivating complex / animal organ morphogenesis / Formation of the beta-catenin:TCF transactivating complex / negative regulation of canonical Wnt signaling pathway / NOTCH1 Intracellular Domain Regulates Transcription ...Repression of WNT target genes / beta-catenin-TCF complex / negative regulation of Wnt signaling pathway / negative regulation of anoikis / negative regulation of canonical NF-kappaB signal transduction / Deactivation of the beta-catenin transactivating complex / animal organ morphogenesis / Formation of the beta-catenin:TCF transactivating complex / negative regulation of canonical Wnt signaling pathway / NOTCH1 Intracellular Domain Regulates Transcription / Wnt signaling pathway / transcription corepressor activity / DNA-binding transcription factor binding / transcription regulator complex / negative regulation of DNA-templated transcription / positive regulation of gene expression / signal transduction / nucleoplasm / identical protein binding / nucleus / cytosol
Similarity search - Function
Groucho/TLE, N-terminal Q-rich domain / Groucho/TLE N-terminal Q-rich domain / Groucho/transducin-like enhancer / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat ...Groucho/TLE, N-terminal Q-rich domain / Groucho/TLE N-terminal Q-rich domain / Groucho/transducin-like enhancer / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Transducin-like enhancer protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å
AuthorsChodaparambil, J.V. / Weis, W.I.
CitationJournal: Embo J. / Year: 2014
Title: Molecular functions of the TLE tetramerization domain in Wnt target gene repression.
Authors: Chodaparambil, J.V. / Pate, K.T. / Hepler, M.R. / Tsai, B.P. / Muthurajan, U.M. / Luger, K. / Waterman, M.L. / Weis, W.I.
History
DepositionJan 25, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 9, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 16, 2014Group: Database references

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Transducin-like enhancer protein 1
B: Transducin-like enhancer protein 1
C: Transducin-like enhancer protein 1
D: Transducin-like enhancer protein 1


Theoretical massNumber of molelcules
Total (without water)73,7084
Polymers73,7084
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12940 Å2
ΔGint-141 kcal/mol
Surface area29140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)49.586, 94.908, 130.207
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

-
Components

#1: Protein
Transducin-like enhancer protein 1 / E(Sp1) homolog / Enhancer of split groucho-like protein 1 / ESG1


Mass: 18427.002 Da / Num. of mol.: 4 / Fragment: TLE Q-domain (UNP residues 1-156)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TLE, TLE1 / Plasmid: pPROEX-HTB / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q04724

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.08 Å3/Da / Density % sol: 40.82 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 200mM sodium thiocyanate, 15% PEG3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

-
Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03 Å
DetectorType: MAR CCD 130 mm / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03 Å / Relative weight: 1
ReflectionResolution: 4→76 Å / Num. obs: 8169 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.2 % / Biso Wilson estimate: 160.69 Å2 / Rmerge(I) obs: 0.116 / Net I/σ(I): 4.9

-
Processing

Software
NameVersionClassificationNB
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.14data extraction
Blu-Icedata collection
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 4→53.686 Å / FOM work R set: 0.5215 / SU ML: 0.84 / σ(F): 1.14 / Phase error: 49.14 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.3474 549 10.01 %random
Rwork0.2874 ---
obs0.2939 5484 98.05 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 291.08 Å2 / Biso mean: 132.2 Å2 / Biso min: 20 Å2
Refinement stepCycle: LAST / Resolution: 4→53.686 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3512 0 0 0 3512
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0043565
X-RAY DIFFRACTIONf_angle_d0.7834799
X-RAY DIFFRACTIONf_chiral_restr0.051534
X-RAY DIFFRACTIONf_plane_restr0.003629
X-RAY DIFFRACTIONf_dihedral_angle_d17.8941355
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
4-4.40250.44251360.382212211357100
4.4025-5.03910.37071340.32021208134298
5.0391-6.34710.42891360.35781229136599
6.3471-53.69120.29641430.22951277142096
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.5444-0.69390.73174.89261.12530.7996-1.00221.6735-0.6974-1.0156-0.9372-0.355-0.11490.2569-1.69161.5052-1.69540.63962.835-0.35890.6852-7.064.4097-24.9351
23.20220.5958-0.65090.339-0.01870.10310.6452-0.17370.4172-0.28590.4292-0.173-1.96290.27940.34011.6425-0.05620.26730.6414-0.15080.7856-16.2615-9.2995-73.3833
31.18-0.18481.49981.06750.03522.1534-1.2892.7543-1.4823-1.8010.8051-0.8541-2.098-0.2137-1.31741.5734-0.09120.32621.8961-0.4221.0283-6.7075-17.31-112.6174
41.17191.1942-0.29691.74110.10721.8278-0.126-0.69440.0495-0.4738-0.8517-1.0156-0.5091-0.6541-1.73411.12420.88060.08041.37090.02990.8511-10.46650.7373-92.1707
5-1.2633-0.0744-0.07820.051-0.30850.7335-1.04710.09060.1072-0.8109-0.21780.447-1.6655-0.2873-0.06170.969-0.1023-0.23091.3763-0.36480.6533-11.90729.530123.4879
64.24031.3258-1.3025.9866-0.49611.7450.8075-1.5063-0.24891.310.780.47960.21960.44111.8810.21730.9873-0.18620.9607-0.30520.5901-2.338415.356671.9516
70.43680.3357-0.01752.24851.92711.92770.365-0.76720.97060.75451.616-3.17610.84951.30131.0891.33140.57970.04141.48420.01481.5198-10.6451.169152.614
80.18941.2237-0.26770.72810.21711.93040.04390.20830.09710.0331-0.3589-0.0105-0.9254-0.37130.49220.73370.30510.03780.8054-0.04660.8256-13.6469-8.8588-62.9997
92.6611.1896-1.35320.5601-0.77121.2379-0.73170.3844-0.749-1.1311-0.9885-0.00170.7434-0.9069-2.61511.8468-0.1443-0.23531.655-0.43310.9685-21.7722-21.7135-103.0661
10-0.01330.72221.60850.27590.36981.6431-0.33110.72670.9181-0.5141-0.2659-0.1557-0.3955-0.0875-0.59761.04460.4202-0.33121.5465-0.67780.8686-10.099511.286822.5893
111.55150.84251.19090.40531.25758.5888-1.1093-0.58341.57370.7288-0.27660.47560.5973-3.7813-1.59180.2710.2311-1.17831.0273-0.127-1.3389-14.744725.4563.2736
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1CHAIN A AND (RESID 21:37)A0
2X-RAY DIFFRACTION2CHAIN A AND (RESID 38:90)A0
3X-RAY DIFFRACTION3CHAIN A AND (RESID 91:116)A0
4X-RAY DIFFRACTION4CHAIN A AND (RESID 117:132)A0
5X-RAY DIFFRACTION5CHAIN B AND (RESID 23:92)B0
6X-RAY DIFFRACTION6CHAIN B AND (RESID 93:117)B0
7X-RAY DIFFRACTION7CHAIN B AND (RESID 118:129)B0
8X-RAY DIFFRACTION8CHAIN C AND (RESID 22:92)C0
9X-RAY DIFFRACTION9CHAIN C AND (RESID 93:131)C0
10X-RAY DIFFRACTION10CHAIN D AND (RESID 22:93)D0
11X-RAY DIFFRACTION11CHAIN D AND (RESID 94:129)D0

+
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://pdbjlvh1.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