+Open data
-Basic information
Entry | Database: PDB / ID: 5z2q | |||||||||
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Title | Vgll1-TEAD4 core complex | |||||||||
Components |
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Keywords | TRANSCRIPTION / TEAD / Transcription factor / co-regulator / Vgll1 / Vestigial | |||||||||
Function / homology | Function and homology information RUNX3 regulates YAP1-mediated transcription / YAP1- and WWTR1 (TAZ)-stimulated gene expression / trophectodermal cell fate commitment / : / hippo signaling / blastocyst formation / cell fate specification / positive regulation of stem cell population maintenance / cell fate commitment / embryonic organ development ...RUNX3 regulates YAP1-mediated transcription / YAP1- and WWTR1 (TAZ)-stimulated gene expression / trophectodermal cell fate commitment / : / hippo signaling / blastocyst formation / cell fate specification / positive regulation of stem cell population maintenance / cell fate commitment / embryonic organ development / embryo implantation / protein-DNA complex / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / transcription regulator complex / sequence-specific DNA 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 / DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.74 Å | |||||||||
Authors | Pobbati, A.V. / Song, H. | |||||||||
Citation | Journal: Structure / Year: 2012 Title: Structural and functional similarity between the Vgll1-TEAD and the YAP-TEAD complexes. Authors: Pobbati, A.V. / Chan, S.W. / Lee, I. / Song, H. / Hong, W. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5z2q.cif.gz | 222.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5z2q.ent.gz | 179.3 KB | Display | PDB format |
PDBx/mmJSON format | 5z2q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z2/5z2q ftp://data.pdbj.org/pub/pdb/validation_reports/z2/5z2q | HTTPS FTP |
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-Related structure data
Related structure data | 3juaS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Refine code: 0
NCS ensembles :
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-Components
-Transcription cofactor vestigial-like protein ... , 2 types, 2 molecules CD
#1: Protein/peptide | Mass: 5600.120 Da / Num. of mol.: 1 / Fragment: UNP residues 20-53 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Vgll1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q99NC0 |
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#2: Protein/peptide | Mass: 5757.314 Da / Num. of mol.: 1 / Fragment: UNP residues 20-54 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Vgll1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q99NC0 |
-Transcriptional enhancer factor TEF- ... , 2 types, 2 molecules AB
#3: Protein | Mass: 26490.045 Da / Num. of mol.: 1 / Fragment: UNP residues 210-426 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tead4, Tcf13r1, Tef3, Tefr1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q62296 |
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#4: Protein | Mass: 26718.291 Da / Num. of mol.: 1 / Fragment: UNP residues 210-426 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tead4, Tcf13r1, Tef3, Tefr1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q62296 |
-Non-polymers , 2 types, 10 molecules
#5: Chemical | ChemComp-PO4 / |
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#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.46 Å3/Da / Density % sol: 72.41 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.9 / Details: 1M phosphate buffer |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 / Wavelength: 0.99 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 3, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | Resolution: 2.74→98.67 Å / Num. obs: 28983 / % possible obs: 99.7 % / Redundancy: 5.6 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 2.7 |
Reflection shell | Resolution: 2.74→2.81 Å / Rmerge(I) obs: 0.58 / Num. unique obs: 1974 / % possible all: 98.87 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: TEAD4 in 3JUA Resolution: 2.74→98.67 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.923 / SU B: 23.465 / SU ML: 0.205 / Cross valid method: THROUGHOUT / ESU R: 0.348 / ESU R Free: 0.268 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 84.267 Å2
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Refinement step | Cycle: 1 / Resolution: 2.74→98.67 Å
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Refine LS restraints |
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