An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex.

Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE, Nucleic Acids Res (2020) Europe PMC

SASDJ72 – DNA Ligase IIIα monomer/dimer

DNA ligase 3 (DNA ligase III alpha)
MWexperimental 150 kDa
VPorod 240 nm3
log I(s) 1.69×102 1.69×101 1.69×100 1.69×10-1
DNA ligase 3 (DNA ligase III alpha) small angle scattering data  s, nm-1
ln I(s)
DNA ligase 3 (DNA ligase III alpha) Guinier plot ln 1.69×102 Rg: 6.1 nm 0 (6.1 nm)-2 s2
(sRg)2I(s)/I(0)
DNA ligase 3 (DNA ligase III alpha) Kratky plot 1.104 0 √3 sRg
p(r)
DNA ligase 3 (DNA ligase III alpha) pair distance distribution function Rg: 6.3 nm 0 Dmax: 21 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DNA ligase 3 (DNA ligase III alpha) BILBOMD model
DNA ligase 3 (DNA ligase III alpha) BILBOMD model
Synchrotron SAXS data from solutions of DNA Ligase IIIα in 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.11 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 5 mg/ml were measured at 20°C. Three successive 0.500 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

DNA ligase 3 (DNA ligase III alpha) (LigIIIα)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Other
Mon. MW   102.7 kDa
 
UniProt   P49916 (88-1009)
Sequence   FASTA