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- PDB-8xwc: Crystal structure of human 8-oxoguanine glycosylase K249H mutant ... -

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Basic information

Entry
Database: PDB / ID: 8xwc
TitleCrystal structure of human 8-oxoguanine glycosylase K249H mutant bound to the substrate 8-oxoguanine DNA at pH 8.0 under 277 K
Components
  • DNA (5'-D(*AP*GP*CP*GP*TP*CP*CP*AP*(8OG)P*GP*TP*CP*TP*AP*CP*C)-3')
  • DNA (5'-D(P*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3')
  • N-glycosylase/DNA lyase
KeywordsDNA/HYDROLASE / DNA / repair / LYASE / DNA-HYDROLASE complex
Function / homology
Function and homology information


Defective OGG1 Substrate Binding / Defective OGG1 Substrate Processing / Defective OGG1 Localization / depurination / negative regulation of double-strand break repair via single-strand annealing / oxidized purine nucleobase lesion DNA N-glycosylase activity / base-excision repair, AP site formation / depyrimidination / 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity / Displacement of DNA glycosylase by APEX1 ...Defective OGG1 Substrate Binding / Defective OGG1 Substrate Processing / Defective OGG1 Localization / depurination / negative regulation of double-strand break repair via single-strand annealing / oxidized purine nucleobase lesion DNA N-glycosylase activity / base-excision repair, AP site formation / depyrimidination / 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity / Displacement of DNA glycosylase by APEX1 / positive regulation of gene expression via chromosomal CpG island demethylation / oxidized purine DNA binding / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / DNA-(apurinic or apyrimidinic site) lyase / cellular response to reactive oxygen species / nucleotide-excision repair / response to radiation / base-excision repair / nuclear matrix / endonuclease activity / microtubule binding / response to oxidative stress / damaged DNA binding / nuclear speck / mitochondrial matrix / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA damage response / regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / mitochondrion / DNA binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
8-oxoguanine DNA-glycosylase / 8-oxoguanine DNA glycosylase, N-terminal / : / 8-oxoguanine DNA glycosylase, N-terminal domain / HhH-GPD superfamily base excision DNA repair protein / Helix-hairpin-helix, base-excision DNA repair, C-terminal / HhH-GPD domain / endonuclease III / DNA glycosylase
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / DNA / DNA (> 10) / N-glycosylase/DNA lyase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å
AuthorsUnno, M. / Koga, M. / Minowa, N. / Komuro, S. / Tanaka, Y.
Funding support Japan, 4items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)22K05320 Japan
Japan Society for the Promotion of Science (JSPS)19K05705 Japan
Japan Society for the Promotion of Science (JSPS)19K06507 Japan
Japan Society for the Promotion of Science (JSPS)16K07261 Japan
CitationJournal: To Be Published
Title: Active residue mutation of hOGG1 provides a novel active mutant with an alternative reaction pathway
Authors: Unno, M. / Morikawa, M. / Sychovsky, V. / Koga, M. / Minowa, N. / Komuro, S. / Fukuta, M. / Tshuyuguchi, F. / Inamura, R. / Mano, H. / Nakashima, K. / Okamoto, Y. / Saito, T. / Hattori, Y. / Tanaka, Y.
History
DepositionJan 16, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 23, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: DNA (5'-D(*AP*GP*CP*GP*TP*CP*CP*AP*(8OG)P*GP*TP*CP*TP*AP*CP*C)-3')
D: DNA (5'-D(P*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3')
A: N-glycosylase/DNA lyase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,6409
Polymers47,2113
Non-polymers4306
Water7,800433
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5140 Å2
ΔGint-37 kcal/mol
Surface area17870 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.808, 69.544, 87.955
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

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Components

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DNA chain , 2 types, 2 molecules CD

#1: DNA chain DNA (5'-D(*AP*GP*CP*GP*TP*CP*CP*AP*(8OG)P*GP*TP*CP*TP*AP*CP*C)-3')


Mass: 4875.155 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#2: DNA chain DNA (5'-D(P*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3')


Mass: 4635.010 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)

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Protein , 1 types, 1 molecules A

#3: Protein N-glycosylase/DNA lyase


Mass: 37700.637 Da / Num. of mol.: 1 / Mutation: K249H
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: OGG1, MMH, MUTM, OGH1 / Production host: Escherichia coli (E. coli)
References: UniProt: O15527, Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds, DNA-(apurinic or apyrimidinic site) lyase

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Non-polymers , 5 types, 439 molecules

#4: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: Na
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 433 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationN

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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 Å3/Da / Density % sol: 38.56 %
Crystal growTemperature: 277 K / Method: vapor diffusion / Details: Sodium cacodylate, MgCl2, PEG 4000, glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 20, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.45→46.2 Å / Num. obs: 67334 / % possible obs: 99.2 % / Redundancy: 6 % / Biso Wilson estimate: 12.15 Å2 / CC1/2: 1 / Net I/σ(I): 35.6
Reflection shellResolution: 1.45→1.47 Å / Num. unique obs: 3039 / CC1/2: 0.967

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
PHENIX1.20.1_4487refinement
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.45→43.98 Å / SU ML: 0.1049 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 16.0709
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1786 3315 4.93 %
Rwork0.1541 63948 -
obs0.1553 67263 99.13 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 17.07 Å2
Refinement stepCycle: LAST / Resolution: 1.45→43.98 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2497 634 27 433 3591
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01633406
X-RAY DIFFRACTIONf_angle_d1.54694777
X-RAY DIFFRACTIONf_chiral_restr0.1007513
X-RAY DIFFRACTIONf_plane_restr0.0149514
X-RAY DIFFRACTIONf_dihedral_angle_d22.8438683
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.45-1.470.20361250.16482402X-RAY DIFFRACTION90.54
1.47-1.490.19281260.16232476X-RAY DIFFRACTION93.43
1.49-1.520.1781260.16052605X-RAY DIFFRACTION97.22
1.52-1.540.18291450.15332607X-RAY DIFFRACTION98.85
1.54-1.570.21621420.15332617X-RAY DIFFRACTION99.93
1.57-1.60.18771580.14822650X-RAY DIFFRACTION100
1.6-1.630.17891540.15412656X-RAY DIFFRACTION99.96
1.63-1.660.20961500.15112646X-RAY DIFFRACTION100
1.66-1.70.1951300.15422662X-RAY DIFFRACTION100
1.7-1.740.19271560.16072642X-RAY DIFFRACTION99.96
1.74-1.780.17361260.15782685X-RAY DIFFRACTION100
1.78-1.830.1731290.15592695X-RAY DIFFRACTION99.96
1.83-1.880.18381440.14582648X-RAY DIFFRACTION99.96
1.88-1.940.16231390.15122677X-RAY DIFFRACTION99.96
1.94-2.010.17921210.15492674X-RAY DIFFRACTION100
2.01-2.090.18171390.15862676X-RAY DIFFRACTION100
2.09-2.190.19621320.15292706X-RAY DIFFRACTION100
2.19-2.30.17671580.15412668X-RAY DIFFRACTION99.93
2.3-2.450.16021270.15372722X-RAY DIFFRACTION99.89
2.45-2.630.16791430.1592691X-RAY DIFFRACTION99.93
2.63-2.90.18791260.16662741X-RAY DIFFRACTION99.97
2.9-3.320.1761270.15882752X-RAY DIFFRACTION99.93
3.32-4.180.17211390.13752763X-RAY DIFFRACTION99.66
4.18-43.980.17231530.15572887X-RAY DIFFRACTION99.87

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