MACROMOLECULE TYPE: heterocomplex

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

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

SASDHE5 – Rel Homology Domain of p50/RelA bound to IFN kB site DNA

NF-kappa-B p105 subunit 39-350Transcription factor p65 19-321IFN kB DNA experimental SAS data
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 IFN kB DNA Kratky plot
Sample: NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Transcription factor p65 19-321 monomer, 35 kDa Mus musculus protein
IFN kB DNA monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 4.3 nm
Dmax 13.0 nm
VolumePorod 237 nm3

SASDHF5 – Rel Homology Domain of p50/RelA bound to Urokinase kB site DNA

NF-kappa-B p105 subunit 39-350Transcription factor p65 19-321Urokinase kB experimental SAS data
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 Urokinase kB Kratky plot
Sample: NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Transcription factor p65 19-321 monomer, 35 kDa Mus musculus protein
Urokinase kB monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 4.1 nm
Dmax 13.0 nm
VolumePorod 244 nm3

SASDHG5 – Nuclear factor kB p50/RelA bound to IFN kB site DNA

Transcription factor p65 19-549NF-kappa-B p105 subunit 39-350IFN kB DNA experimental SAS data
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 IFN kB DNA Kratky plot
Sample: Transcription factor p65 19-549 monomer, 58 kDa Mus musculus protein
NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
IFN kB DNA monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 4
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 5.1 nm
Dmax 18.9 nm
VolumePorod 314 nm3

SASDHH5 – Nuclear factor kB p50/RelA bound to Urokinase kB site DNA

Transcription factor p65 19-549NF-kappa-B p105 subunit 39-350Urokinase kB experimental SAS data
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 Urokinase kB Kratky plot
Sample: Transcription factor p65 19-549 monomer, 58 kDa Mus musculus protein
NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Urokinase kB monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 4
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 4.7 nm
Dmax 17.5 nm
VolumePorod 201 nm3

SASDLS7 – Mycobacterium phage TipsytheTRex immunity repressor bound to DNA

Immunity repressor21mer dsDNA experimental SAS data
BILBOMD model
Sample: Immunity repressor monomer, 21 kDa Mycobacterium phage TipsytheTRex protein
21mer dsDNA monomer, 13 kDa DNA
Buffer: 20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 10
A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence. Nat Commun 13(1):4105 (2022)
McGinnis RJ, Brambley CA, Stamey B, Green WC, Gragg KN, Cafferty ER, Terwilliger TC, Hammel M, Hollis TJ, Miller JM, Gainey MD, Wallen JR
RgGuinier 2.3 nm
Dmax 7.4 nm
VolumePorod 41 nm3

SASDML3 – Mycobacterium phage TipsytheTRex immunity repressor bound to 24mer DNA

Immunity repressor24mer dsDNA experimental SAS data
BILBOMD model
Sample: Immunity repressor monomer, 21 kDa Mycobacterium phage TipsytheTRex protein
24mer dsDNA monomer, 15 kDa DNA
Buffer: 20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 10
A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence. Nat Commun 13(1):4105 (2022)
McGinnis RJ, Brambley CA, Stamey B, Green WC, Gragg KN, Cafferty ER, Terwilliger TC, Hammel M, Hollis TJ, Miller JM, Gainey MD, Wallen JR
RgGuinier 2.4 nm
Dmax 9.0 nm
VolumePorod 43 nm3

SASDMM3 – Mycobacterium phage TipsytheTRex immunity repressor mixed with 13mer DNA

Immunity repressor13mer dsDNA experimental SAS data
BILBOMD model
Sample: Immunity repressor monomer, 21 kDa Mycobacterium phage TipsytheTRex protein
13mer dsDNA monomer, 8 kDa DNA
Buffer: 20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 10
A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence. Nat Commun 13(1):4105 (2022)
McGinnis RJ, Brambley CA, Stamey B, Green WC, Gragg KN, Cafferty ER, Terwilliger TC, Hammel M, Hollis TJ, Miller JM, Gainey MD, Wallen JR
RgGuinier 2.0 nm
Dmax 8.5 nm
VolumePorod 18 nm3

SASDKV9 – Transcription factors USF1 and NF-Y bound to a CCAAT DNA box(48bp)

Upstream stimulatory factor 1Nuclear transcription factor Y subunit alphaNuclear transcription factor Y subunit betaNuclear transcription factor Y subunit gammaDNA 48bp experimental SAS data
CORAL model
Sample: Upstream stimulatory factor 1 dimer, 50 kDa Homo sapiens protein
Nuclear transcription factor Y subunit alpha monomer, 10 kDa Homo sapiens protein
Nuclear transcription factor Y subunit beta monomer, 11 kDa Homo sapiens protein
Nuclear transcription factor Y subunit gamma monomer, 11 kDa Homo sapiens protein
DNA 48bp monomer, 30 kDa DNA
Buffer: 100 mM cacodylate buffer, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 14
The USR domain of USF1 mediates NF-Y interactions and cooperative DNA binding International Journal of Biological Macromolecules (2021)
Bernardini A, Lorenzo M, Chaves-Sanjuan A, Swuec P, Pigni M, Saad D, Konarev P, Graewert M, Valentini E, Svergun D, Nardini M, Mantovani R, Gnesutta N
RgGuinier 4.8 nm
Dmax 17.0 nm
VolumePorod 155 nm3