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- PDB-4l7x: Crystal structure of the DIDO PHD finger in complex with H3K4me3 -

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Basic information

Entry
Database: PDB / ID: 4l7x
TitleCrystal structure of the DIDO PHD finger in complex with H3K4me3
Components
  • Death-inducer obliterator 1
  • Histone H3 peptide
KeywordsCELL CYCLE / GENE REGULATION / mitosis / Chromatin
Function / homology
Function and homology information


Chromatin modifying enzymes / telomere organization / Meiotic synapsis / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / epigenetic regulation of gene expression / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / Condensation of Prophase Chromosomes ...Chromatin modifying enzymes / telomere organization / Meiotic synapsis / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / epigenetic regulation of gene expression / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / apoptotic signaling pathway / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / HDMs demethylate histones / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / spindle / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / nucleosome / nucleosome assembly / chromatin organization / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / gene expression / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / cadherin binding / protein heterodimerization activity / Amyloid fiber formation / DNA-templated transcription / protein-containing complex / DNA binding / RNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / metal ion binding / cytoplasm
Similarity search - Function
Death-inducer obliterator 1 / Spen paralogue and orthologue SPOC, C-terminal / SPOC domain / Transcription factor S-II (TFIIS), central domain / Domain in the central regions of transcription elongation factor S-II (and elsewhere) / Transcription elongation factor S-II, central domain / Transcription elongation factor S-II, central domain superfamily / TFIIS central domain profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 ...Death-inducer obliterator 1 / Spen paralogue and orthologue SPOC, C-terminal / SPOC domain / Transcription factor S-II (TFIIS), central domain / Domain in the central regions of transcription elongation factor S-II (and elsewhere) / Transcription elongation factor S-II, central domain / Transcription elongation factor S-II, central domain superfamily / TFIIS central domain profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, PHD-type, conserved site / PHD-finger / Zinc finger PHD-type signature. / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Zinc finger, FYVE/PHD-type / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Zinc finger, RING/FYVE/PHD-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Histone H3.1 / Death-inducer obliterator 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.35 Å
AuthorsTong, Q. / Gatchalian, J. / Kutateladze, T.G.
CitationJournal: Cell Rep / Year: 2013
Title: Dido3 PHD Modulates Cell Differentiation and Division.
Authors: Gatchalian, J. / Futterer, A. / Rothbart, S.B. / Tong, Q. / Rincon-Arano, H. / Sanchez de Diego, A. / Groudine, M. / Strahl, B.D. / Martinez-A, C. / van Wely, K.H. / Kutateladze, T.G.
History
DepositionJun 14, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 24, 2013Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Death-inducer obliterator 1
U: Histone H3 peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)8,7624
Polymers8,6312
Non-polymers1312
Water1,33374
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1240 Å2
ΔGint-4 kcal/mol
Surface area4300 Å2
MethodPISA
Unit cell
Length a, b, c (Å)40.820, 40.820, 80.620
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein Death-inducer obliterator 1 / DIO-1 / hDido1 / Death-associated transcription factor 1 / DATF-1


Mass: 7280.341 Da / Num. of mol.: 1 / Fragment: PHD-type zinc finger domain residues 266-325
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DIDO1, C20orf158, DATF1, KIAA0333 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9BTC0
#2: Protein/peptide Histone H3 peptide / H3K4me3 peptide


Mass: 1350.568 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Peptide was synthesized. / Source: (synth.) Homo sapiens (human) / References: UniProt: P68431*PLUS
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 74 / 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: 1.95 Å3/Da / Density % sol: 36.78 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 0.1M HEPES pH8, 30% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 26, 2013
RadiationMonochromator: Si-111 double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.35→28.7 Å / Num. obs: 28593 / % possible obs: 100 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2
Reflection shellResolution: 1.35→1.4 Å / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIXmodel building
PHENIX(phenix.refine: 1.8.1_1168)refinement
MOSFLMdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 1.35→28.682 Å / SU ML: 0.07 / σ(F): 1.35 / Phase error: 12.82 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1422 1425 4.98 %RANDOM
Rwork0.1324 ---
all0.14 28593 --
obs0.1329 28593 99.96 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.35→28.682 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms518 0 2 74 594
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.007528
X-RAY DIFFRACTIONf_angle_d1.169713
X-RAY DIFFRACTIONf_dihedral_angle_d15.32201
X-RAY DIFFRACTIONf_chiral_restr0.07672
X-RAY DIFFRACTIONf_plane_restr0.00796
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.35-1.39830.18111460.14692711X-RAY DIFFRACTION100
1.3983-1.45420.16821160.12662758X-RAY DIFFRACTION100
1.4542-1.52040.16581620.11112704X-RAY DIFFRACTION100
1.5204-1.60060.15861490.10612696X-RAY DIFFRACTION100
1.6006-1.70090.11931700.10222700X-RAY DIFFRACTION100
1.7009-1.83220.12391430.10782693X-RAY DIFFRACTION100
1.8322-2.01650.14111280.11212734X-RAY DIFFRACTION100
2.0165-2.30820.13071360.1192731X-RAY DIFFRACTION100
2.3082-2.90760.1351360.1482722X-RAY DIFFRACTION100
2.9076-28.68850.14751390.15042719X-RAY DIFFRACTION100

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