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- PDB-1khc: Crystal Structure of the PWWP Domain of Mammalian DNA Methyltrans... -

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Basic information

Entry
Database: PDB / ID: 1khc
TitleCrystal Structure of the PWWP Domain of Mammalian DNA Methyltransferase Dnmt3b
ComponentsDNA cytosine-5 methyltransferase 3B2
KeywordsTRANSFERASE / Five beta-sheets barrel followed by Five-helix bundle
Function / homology
Function and homology information


: / DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates / : / heterochromatin => GO:0000792 / : / SUMOylation of DNA methylation proteins / DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates / : / PRC2 methylates histones and DNA / epigenetic programming of gene expression ...: / DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates / : / heterochromatin => GO:0000792 / : / SUMOylation of DNA methylation proteins / DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates / : / PRC2 methylates histones and DNA / epigenetic programming of gene expression / DNA (cytosine-5-)-methyltransferase / DNA (cytosine-5-)-methyltransferase activity / DNA methylation-dependent heterochromatin formation / protein-containing complex localization / : / negative regulation of gene expression, epigenetic / : / chromosome, centromeric region / heterochromatin / positive regulation of neuron differentiation / methyltransferase activity / cellular response to amino acid stimulus / histone deacetylase binding / transcription corepressor activity / negative regulation of DNA-templated transcription / chromatin binding / positive regulation of gene expression / negative regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / metal ion binding / nucleus / cytoplasm
Similarity search - Function
PWWP, helical domain / DNA (cytosine-5)-methyltransferase 3B, ADD domain / DNMT3, cysteine rich ADD domain / Cysteine rich ADD domain in DNMT3 / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / ADD domain / ADD domain profile. / DNA methylase, C-5 cytosine-specific, active site / C-5 cytosine-specific DNA methylases active site. / C-5 cytosine-specific DNA methylase (Dnmt) domain profile. ...PWWP, helical domain / DNA (cytosine-5)-methyltransferase 3B, ADD domain / DNMT3, cysteine rich ADD domain / Cysteine rich ADD domain in DNMT3 / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / ADD domain / ADD domain profile. / DNA methylase, C-5 cytosine-specific, active site / C-5 cytosine-specific DNA methylases active site. / C-5 cytosine-specific DNA methylase (Dnmt) domain profile. / C-5 cytosine methyltransferase / C-5 cytosine-specific DNA methylase / SH3 type barrels. - #140 / domain with conserved PWWP motif / PWWP domain / PWWP domain profile. / PWWP domain / Zinc finger, FYVE/PHD-type / SH3 type barrels. / Roll / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
DNA (cytosine-5)-methyltransferase 3B
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / MAD / Resolution: 1.8 Å
AuthorsQiu, C. / Sawada, K. / Zhang, X. / Cheng, X.
CitationJournal: Nat.Struct.Biol. / Year: 2002
Title: The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds.
Authors: Qiu, C. / Sawada, K. / Zhang, X. / Cheng, X.
History
DepositionNov 29, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 27, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 16, 2011Group: Atomic model
Revision 1.4Feb 14, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 600HETEROGEN THE AUTHORS WERE UNABLE TO FIGURE OUT THE IDENTITY OF THE MOLECULES LABELED AS "UNX" FROM ...HETEROGEN THE AUTHORS WERE UNABLE TO FIGURE OUT THE IDENTITY OF THE MOLECULES LABELED AS "UNX" FROM THE ELECTRON DENSITY.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: DNA cytosine-5 methyltransferase 3B2


Theoretical massNumber of molelcules
Total (without water)16,67023
Polymers16,6701
Non-polymers022
Water2,918162
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)52.750, 52.750, 186.860
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522
Components on special symmetry positions
IDModelComponents
11A-49-

HOH

21A-140-

HOH

31A-150-

HOH

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Components

#1: Protein DNA cytosine-5 methyltransferase 3B2


Mass: 16670.039 Da / Num. of mol.: 1 / Fragment: PWWP domain (residues 219-365)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Dnmt3b / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: O88509, DNA (cytosine-5-)-methyltransferase
#2: Chemical...
ChemComp-UNX / UNKNOWN ATOM OR ION


Num. of mol.: 22 / Source method: obtained synthetically
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 162 / 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: 2.25 Å3/Da / Density % sol: 48 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 30% PEG 8000, 0.1M sodium cacodylate, 0.2M sodium acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Crystal grow
*PLUS
Temperature: 16 ℃ / pH: 7
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
124 mg/mlprotein1drop
220 mMHEPES1droppH7.0
3200 mM1dropNaCl
41 mMEDTA1drop
55 %(v/v)glycerol1drop
630 %(w/v)PEG80001reservoir
7200 mMsodium acetate1reservoir
8100 mMsodium cacodylate1reservoirpH6.5

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
1951
21
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 27, 2000
RadiationMonochromator: confocal multilayer mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 1.8→20 Å / Num. all: 15308 / Num. obs: 15308 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.5 % / Rmerge(I) obs: 0.038 / Net I/σ(I): 23.6
Reflection shellResolution: 1.8→1.83 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.148 / Mean I/σ(I) obs: 9.4 / % possible all: 94.3
Reflection
*PLUS
Num. measured all: 145433
Reflection shell
*PLUS
% possible obs: 94.3 %

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Processing

Software
NameClassification
SOLVEphasing
RESOLVEmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
RESOLVEphasing
RefinementMethod to determine structure: MAD / Resolution: 1.8→20 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.237 1477 10 %random
Rwork0.19 ---
obs-14656 97.1 %-
Displacement parametersBiso mean: 15.442 Å2
Refinement stepCycle: LAST / Resolution: 1.8→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1057 0 22 162 1241
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.006
X-RAY DIFFRACTIONx_angle_deg1.3
X-RAY DIFFRACTIONx_dihedral_angle_d24.219
X-RAY DIFFRACTIONx_improper_angle_d0.615
LS refinement shellResolution: 1.8→1.88 Å / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rfree0.282 166 11.4 %
Rwork0.275 1450 -
obs--87.7 %
Refinement
*PLUS
Lowest resolution: 20 Å / % reflection Rfree: 10 % / Rfactor obs: 0.19 / Rfactor Rwork: 0.19
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg24.219
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg0.615
LS refinement shell
*PLUS
Highest resolution: 1.8 Å / Rfactor Rfree: 0.282 / % reflection Rfree: 11.4 % / Rfactor Rwork: 0.275

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