- PDB-1dpu: SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLE... -
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Basic information
Entry
Database: PDB / ID: 1dpu
Title
SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)
Components
REPLICATION PROTEIN A (RPA32) C-TERMINAL DOMAIN
URACIL DNA GLYCOSYLASE (UNG2)
Keywords
DNA BINDING PROTEIN / PROTEIN-PEPTIDE COMPLEX / DNA REPAIR
Function / homology
Function and homology information
protein localization to chromosome / DNA replication factor A complex / base-excision repair, AP site formation via deaminated base removal / uracil-DNA glycosylase / depyrimidination / Displacement of DNA glycosylase by APEX1 / regulation of DNA damage checkpoint / Removal of the Flap Intermediate / isotype switching / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) ...protein localization to chromosome / DNA replication factor A complex / base-excision repair, AP site formation via deaminated base removal / uracil-DNA glycosylase / depyrimidination / Displacement of DNA glycosylase by APEX1 / regulation of DNA damage checkpoint / Removal of the Flap Intermediate / isotype switching / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / uracil DNA N-glycosylase activity / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / regulation of double-strand break repair via homologous recombination / telomeric DNA binding / Presynaptic phase of homologous DNA pairing and strand exchange / ribosomal small subunit binding / Activation of the pre-replicative complex / Regulation of HSF1-mediated heat shock response / PCNA-Dependent Long Patch Base Excision Repair / HSF1 activation / somatic hypermutation of immunoglobulin genes / mismatch repair / Activation of ATR in response to replication stress / mitotic G1 DNA damage checkpoint signaling / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / telomere maintenance / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / Chromatin modifications during the maternal to zygotic transition (MZT) / nucleotide-excision repair / Fanconi Anemia Pathway / Recognition of DNA damage by PCNA-containing replication complex / Termination of translesion DNA synthesis / Translesion Synthesis by POLH / double-strand break repair via homologous recombination / base-excision repair / G2/M DNA damage checkpoint / HDR through Homologous Recombination (HRR) / PML body / Dual Incision in GG-NER / Meiotic recombination / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / single-stranded DNA binding / Processing of DNA double-strand break ends / protein phosphatase binding / DNA replication / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / chromosome, telomeric region / nuclear body / ubiquitin protein ligase binding / chromatin / negative regulation of apoptotic process / enzyme binding / mitochondrion / nucleoplasm / nucleus Similarity search - Function
Replication factor A protein 2 / Replication protein A, C-terminal / Replication protein A C terminal / Replication factor A protein-like / Uracil-DNA glycosylase family 1 / UreE urease accessory protein, C-terminal domain / Uracil DNA glycosylase superfamily / Uracil-DNA glycosylase, active site / Uracil-DNA glycosylase signature. / Uracil-DNA glycosylase-like ...Replication factor A protein 2 / Replication protein A, C-terminal / Replication protein A C terminal / Replication factor A protein-like / Uracil-DNA glycosylase family 1 / UreE urease accessory protein, C-terminal domain / Uracil DNA glycosylase superfamily / Uracil-DNA glycosylase, active site / Uracil-DNA glycosylase signature. / Uracil-DNA glycosylase-like / Uracil DNA glycosylase superfamily / Uracil-DNA glycosylase-like domain superfamily / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold / Orthogonal Bundle / Mainly Alpha Similarity search - Domain/homology
Mass: 10585.656 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN (RESIDUES 172-270) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P15927
#2: Protein/peptide
URACILDNAGLYCOSYLASE (UNG2)
Mass: 1826.222 Da / Num. of mol.: 1 / Fragment: RESIDUES 73-88 / Source method: obtained synthetically Details: THIS PEPTIDE SEQUENCE IS FOUND IN THE NUCLEAR [UNG2(73-88)] AND MITOCHONDRIAL [UNG1(64-79)] FORMS OF HUMAN URACIL-DNA GLYCOSYLASE References: UniProt: P13051
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D NOESY
1
2
1
3D 13C- SEPARATED NOESY
1
3
1
3D 15N- SEPARATED NOESY
1
4
1
DQF- COSY
1
5
1
HNHA
1
6
1
HNHB
1
7
1
HACAHB -COSY
1
8
1
FILTER-EDITED NOESY
1
9
1
DOUBLE-HALF FILTERED NOESY
NMR details
Text: THE STRUCTURE WAS DETERMINED USING DOUBLE- AND TRIPLE-RESONANCE NMR SPECTROSCOPY ***
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Sample preparation
Details
Contents: 1MM RPA32(172-270) U- 15N,13C; 1.2 MM UNG2(73- 88) NA; 25MM PHOSPHATE BUFFER NA; 50MM NACL; 5 MM DTT NA
Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 30
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