SASBDB entries for UniProt ID: P27694

SASDH44 – 3' Complex of XPA-DBD and RPA70AB

UniProt ID: P23025 (98-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (183-420) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: None (None-None) 3-prime Nucleotide Excision Repair Junction Model Substrate
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit3-prime Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
3-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 17 Nov 2
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 3.1 nm
Dmax 9.7 nm
VolumePorod 103 nm3

SASDH54 – 5' Complex of XPA-DBD with RPA70AB

UniProt ID: P23025 (98-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (183-420) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: None (None-None) 5-prime Nucleotide Excision Repair Junction Model Substrate
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit5-prime Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
5-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 4
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 2.9 nm
Dmax 97.0 nm
VolumePorod 87 nm3

SASDPZ3 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 3’ss-ds DNA junction NER substrate

UniProt ID: P23025 (1-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (185-616) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: P15927 (45-270) Replication protein A 32 kDa subunit

UniProt ID: P35244 (1-121) Replication protein A 14 kDa subunit

UniProt ID: None (None-None) 3-prime ss-ds DNA junction NER model substrate
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunitReplication protein A 14 kDa subunit3-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
3-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.3 nm
Dmax 14.7 nm
VolumePorod 189 nm3

SASDP24 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 5’ss-ds DNA junction NER substrate

UniProt ID: P35244 (1-121) Replication protein A 14 kDa subunit

UniProt ID: P23025 (1-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (185-616) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: P15927 (45-270) Replication protein A 32 kDa subunit

UniProt ID: None (None-None) 5-prime ss-ds DNA junction NER model substrate
Replication protein A 14 kDa subunitDNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunit5-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
5-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.6 nm
Dmax 16.5 nm
VolumePorod 220 nm3