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- PDB-3l15: Human Tead2 transcriptional factor -

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Basic information

Entry
Database: PDB / ID: 3l15
TitleHuman Tead2 transcriptional factor
ComponentsTranscriptional enhancer factor TEF-4
KeywordsTRANSCRIPTION / Activator / DNA-binding / Nucleus / Transcription regulation
Function / homology
Function and homology information


TEAD-YAP complex / lateral mesoderm development / RUNX3 regulates YAP1-mediated transcription / notochord development / YAP1- and WWTR1 (TAZ)-stimulated gene expression / paraxial mesoderm development / hippo signaling / regulation of stem cell differentiation / Formation of axial mesoderm / embryonic heart tube morphogenesis ...TEAD-YAP complex / lateral mesoderm development / RUNX3 regulates YAP1-mediated transcription / notochord development / YAP1- and WWTR1 (TAZ)-stimulated gene expression / paraxial mesoderm development / hippo signaling / regulation of stem cell differentiation / Formation of axial mesoderm / embryonic heart tube morphogenesis / vasculogenesis / embryonic organ development / cellular response to retinoic acid / neural tube closure / transcription coactivator binding / sequence-specific double-stranded DNA binding / disordered domain specific binding / protein-containing complex assembly / transcription regulator complex / transcription by RNA polymerase II / 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 / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytosol
Similarity search - Function
Coagulation Factor XIII; Chain A, domain 1 - #80 / TEA/ATTS domain / Transcriptional enhancer factor, metazoa / TEA/ATTS domain superfamily / TEA/ATTS domain / TEA domain signature. / TEA domain profile. / TEA domain / YAP binding domain / YAP binding domain ...Coagulation Factor XIII; Chain A, domain 1 - #80 / TEA/ATTS domain / Transcriptional enhancer factor, metazoa / TEA/ATTS domain superfamily / TEA/ATTS domain / TEA domain signature. / TEA domain profile. / TEA domain / YAP binding domain / YAP binding domain / Coagulation Factor XIII; Chain A, domain 1 / Distorted Sandwich / Mainly Beta
Similarity search - Domain/homology
Transcriptional enhancer factor TEF-4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2 Å
AuthorsTomchick, D.R. / Luo, X. / Tian, W.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 2010
Title: Structural and functional analysis of the YAP-binding domain of human TEAD2.
Authors: Tian, W. / Yu, J. / Tomchick, D.R. / Pan, D. / Luo, X.
#1: Journal: DEV.CELL / Year: 2008
Title: The TEAD/TEF family protein Scalloped mediates transcriptional output of the Hippo growth-regulatory pathway
Authors: Wu, S. / Liu, Y. / Zheng, Y. / Dong, J. / Pan, D.
#2: Journal: J.Biol.Chem. / Year: 2009
Title: TEADs mediate nuclear retention of TAZ to promote oncogenic transformation.
Authors: Chan, S.W. / Lim, C.J. / Loo, L.S. / Chong, Y.F. / Huang, C. / Hong, W.
#3: Journal: Genes Dev. / Year: 2008
Title: TEAD mediates YAP-dependent gene induction and growth control.
Authors: Zhao, B. / Ye, X. / Yu, J. / Li, L. / Li, W. / Li, S. / Lin, J.D. / Wang, C.Y. / Chinnaiyan, A.M. / Lai, Z.C. / Guan, K.L.
History
DepositionDec 10, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 7, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Transcriptional enhancer factor TEF-4
B: Transcriptional enhancer factor TEF-4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,2535
Polymers52,9772
Non-polymers2763
Water2,882160
1
A: Transcriptional enhancer factor TEF-4


Theoretical massNumber of molelcules
Total (without water)26,4881
Polymers26,4881
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Transcriptional enhancer factor TEF-4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,7654
Polymers26,4881
Non-polymers2763
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)121.144, 61.567, 80.472
Angle α, β, γ (deg.)90.00, 117.27, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-154-

HOH

21B-158-

HOH

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Components

#1: Protein Transcriptional enhancer factor TEF-4 / TEA domain family member 2 / TEAD-2


Mass: 26488.354 Da / Num. of mol.: 2 / Fragment: C-terminal residues 217-447
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TEAD2, TEF4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q15562
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 160 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.52 Å3/Da / Density % sol: 51.14 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.4
Details: 0.1 M Tris, 2.5 M Sodium Formate, 100 mM NaCl, 2 mM MgCl2, 1 mM TCEP, 5% (w/v) Glycerol;, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.9798 Å
DetectorType: SBC-3 / Detector: CCD / Date: Nov 19, 2009 / Details: monochromator
RadiationMonochromator: SAGITALLY FOCUSED Si(111) / Protocol: SAD / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9798 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. all: 34385 / Num. obs: 34385 / % possible obs: 96.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obs% possible all
2-2.033.80.71170.9
2.03-2.073.90.74878.8
2.07-2.1140.71693.4
2.11-2.154.40.67797.8
2.15-2.24.90.55698.2
2.2-2.2550.53798.1
2.25-2.315.10.598.3
2.31-2.375.20.42598.5
2.37-2.445.20.42998.4
2.44-2.525.20.34398.6
2.52-2.615.20.28198.7
2.61-2.715.20.2398.8
2.71-2.845.20.19499
2.84-2.995.20.14798.9
2.99-3.175.20.11499.2
3.17-3.425.10.08199.2
3.42-3.765.10.06699.3
3.76-4.315.10.05899.5
4.31-5.4350.05299.6
5.43-504.80.06497.8

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIXrefinement
PDB_EXTRACT3.005data extraction
ADSCQuantumdata collection
HKL-3000data reduction
HKL-3000data scaling
SHELXSphasing
RefinementMethod to determine structure: SAD / Resolution: 2→33.738 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 1.75 / Isotropic thermal model: ISOTROPIC AND TLS / σ(F): 0.19 / Phase error: 27.73 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2445 1878 5.79 %
Rwork0.1885 --
obs0.1918 32458 90.62 %
all-32458 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 54.647 Å2 / ksol: 0.441 e/Å3
Displacement parametersBiso mean: 52.545 Å2
Baniso -1Baniso -2Baniso -3
1-11.024 Å2-0 Å211.577 Å2
2---0.416 Å20 Å2
3----10.608 Å2
Refinement stepCycle: LAST / Resolution: 2→33.738 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3277 0 18 160 3455
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.016605
X-RAY DIFFRACTIONf_angle_d1.05611866
X-RAY DIFFRACTIONf_dihedral_angle_d13.931650
X-RAY DIFFRACTIONf_chiral_restr0.102490
X-RAY DIFFRACTIONf_plane_restr0.005986
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.05320.3576880.29531571X-RAY DIFFRACTION60
2.0532-2.11360.35161140.28252023X-RAY DIFFRACTION78
2.1136-2.18180.30771420.25052234X-RAY DIFFRACTION88
2.1818-2.25970.31391480.21962346X-RAY DIFFRACTION90
2.2597-2.35020.29891480.20182355X-RAY DIFFRACTION92
2.3502-2.45710.24161480.20142387X-RAY DIFFRACTION92
2.4571-2.58660.28161480.19412403X-RAY DIFFRACTION93
2.5866-2.74860.2681480.1872439X-RAY DIFFRACTION95
2.7486-2.96070.24881540.18692489X-RAY DIFFRACTION96
2.9607-3.25850.23881580.17682557X-RAY DIFFRACTION97
3.2585-3.72940.20671590.15952542X-RAY DIFFRACTION99
3.7294-4.69670.18351600.13662590X-RAY DIFFRACTION99
4.6967-33.74260.23861630.20562644X-RAY DIFFRACTION98
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)
10.0612-0.1180.0831-0.0486-0.19170.29920.041-0.34050.05140.25490.11410.3199-0.59420.55190.00140.2384-0.01640.03190.52520.01540.273741.375751.2459-7.1594
20.0857-0.1390.04870.1057-0.0589-0.04980.17240.1510.1715-0.184-0.09420.7786-0.01340.32830.00320.3227-0.11560.14130.6889-0.0960.251153.599854.186-11.4989
30.38290.0788-0.08910.0752-0.26690.1414-0.22070.3187-0.0430.21330.48010.18850.1164-0.1091-00.5438-0.0002-0.00820.51090.08010.346632.040450.0132-22.5143
40.1588-0.1482-0.00250.34470.13040.2184-0.0686-0.0812-0.3575-0.14830.1934-0.0075-0.2626-0.33060.00010.28090.03960.00780.30760.06520.423728.566846.2572-18.219
5-0.07120.0313-0.4321-0.21-0.09150.04470.1349-0.3393-0.1730.12460.2230.222-0.45750.6928-0.00020.3091-0.00060.04380.4894-0.06730.328149.740150.5427-12.5193
60.35280.27660.0973-0.04030.40220.1188-0.20370.149-0.15540.11650.0278-0.04150.6619-0.7056-0.00140.38130.0636-0.00020.27310.03330.305537.51440.319-11.804
7-0.0976-0.0241-0.02350.00390.13280.06350.1787-0.76070.0623-0.3872-0.10130.00070.2860.6301-0.00020.29620.05630.01980.4858-0.05660.245438.194646.88384.8446
80.1447-0.0559-0.0023-0.2930.19220.09510.0095-0.5447-0.08180.1421-0.1150.04720.24310.594600.40980.08610.04290.48840.07660.305252.931143.2822-17.8985
90.9586-0.42520.77560.24850.46780.8029-0.084-0.020.2139-0.15680.21230.1502-0.0218-0.0416-0.00020.27490.08620.0380.11690.01840.273341.064447.6084-20.1469
10-0.0323-0.11790.02090.1687-0.11020.2498-0.36060.38360.3788-0.15260.40090.2166-0.8105-0.2232-0.00120.512-0.00950.06270.18940.03180.320239.425559.0972-19.8723
110.0365-0.1338-0.09780.0010.16750.07570.5419-0.3928-0.17090.1004-0.2868-0.10690.1816-0.2297-0.00020.250.01-0.1550.44610.01610.295951.412416.9051-4.5206
120.2279-0.1558-0.15050.25830.18480.3649-0.08590.32850.22630.19170.10730.05530.8604-0.3229-0.0080.2049-0.1042-0.0490.374-0.04420.256730.626713.7866-16.357
130.25830.3420.51550.09710.30970.1732-0.07350.2845-0.0662-0.30890.3840.10920.1260.5766-0.00010.3367-0.02350.04450.5399-0.04780.380559.379416.8597-17.2437
140.5139-0.1078-0.16461.2195-0.12130.3767-0.2401-0.2504-0.1438-0.71540.0682-0.38540.06670.4923-0.00160.2590.0367-0.00310.36330.02210.293659.680225.4509-14.9036
150.11850.1228-0.07170.3361-0.4518-0.05530.1284-0.13550.0641-0.0337-0.08460.07510.3449-0.15960.00010.3722-0.0502-0.02070.2507-0.03130.257239.552516.5546-15.707
160.2670.65220.37920.7757-0.00660.54420.2276-0.1598-0.0089-0.22440.0948-0.0237-0.64240.71490.01470.33070.04380.00050.2626-0.0290.219648.226329.1359-13.2525
170.19660.1379-0.010.1277-0.21290.1264-0.1272-0.5286-0.0670.0219-0.146-0.0093-0.3102-0.744-0.00010.2803-0.06290.03490.5436-0.02780.276341.339723.19661.0725
180.0048-0.16320.05-0.0464-0.04130.07120.08550.10680.00540.2863-0.330.072-0.1536-0.1569-0.00010.36370.00280.02710.3217-0.02090.27137.306822.0987-26.9183
190.92410.2447-0.31320.2091-0.67660.39350.0125-0.0886-0.0386-0.23480.0042-0.1664-0.0824-0.06180.00010.22830.0532-0.01140.21740.00370.287250.055922.0977-20.028
200.03290.0553-0.3628-0.0019-0.22130.5989-0.3010.0581-0.0913-0.35720.2089-0.03420.4560.1404-0.00010.3640.03220.01170.18790.00310.344251.345411.4788-19.8413
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 222:239)
2X-RAY DIFFRACTION2(chain A and resid 247:253)
3X-RAY DIFFRACTION3(chain A and resid 254:281)
4X-RAY DIFFRACTION4(chain A and resid 282:302)
5X-RAY DIFFRACTION5(chain A and resid 303:334)
6X-RAY DIFFRACTION6(chain A and resid 335:359)
7X-RAY DIFFRACTION7(chain A and resid 360:373)
8X-RAY DIFFRACTION8(chain A and resid 374:392)
9X-RAY DIFFRACTION9(chain A and resid 393:431)
10X-RAY DIFFRACTION10(chain A and resid 432:446)
11X-RAY DIFFRACTION11(chain B and resid 221:233)
12X-RAY DIFFRACTION12(chain B and resid 234:253)
13X-RAY DIFFRACTION13(chain B and resid 254:279)
14X-RAY DIFFRACTION14(chain B and resid 280:302)
15X-RAY DIFFRACTION15(chain B and resid 303:335)
16X-RAY DIFFRACTION16(chain B and resid 336:359)
17X-RAY DIFFRACTION17(chain B and resid 360:376)
18X-RAY DIFFRACTION18(chain B and resid 377:393)
19X-RAY DIFFRACTION19(chain B and resid 394:424)
20X-RAY DIFFRACTION20(chain B and resid 425:446)

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