Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase.

Prakash A, Moharana K, Wallace SS, DoubliƩ S, Nucleic Acids Res 45(5):2897-2909 (2017) PubMed

SASDBB7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to DNA

Endonuclease 8-like 1
dsDNA
MWI(0) 57 kDa
MWexpected 47 kDa
VPorod 92 nm3
log I(s) 3.09×102 3.09×101 3.09×100 3.09×10-1
Endonuclease 8-like 1 dsDNA small angle scattering data  s, nm-1
ln I(s)
Endonuclease 8-like 1 dsDNA Guinier plot ln 3.09×102 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Endonuclease 8-like 1 dsDNA Kratky plot 1.104 0 3 sRg
p(r)
Endonuclease 8-like 1 dsDNA pair distance distribution function Rg: 4.1 nm 0 Dmax: 17.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Endonuclease 8-like 1 dsDNA DAMMIN model

Synchrotron SAXS data from solutions of Human NEI like DNA glycosylase 1 (NEIL1) bound to DNA in 25mM HEPES 100mM NaCl 1mM DTT, pH 7.5 were collected on the 12.3.1 (SIBYLS) camera at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.4 m and at a wavelength of λ = 1.127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 2.1 mg/ml were measured at 10°C. 24 successive 0.200 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 theoretical MW for this NEIL1/DNA complex is 55.8kDa.

Endonuclease 8-like 1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   44.7 kDa
 
UniProt   Q96FI4
Sequence   FASTA
 
dsDNA
Mol. type   DNA
Olig. state   Monomer
Mon. MW   2.4 kDa
Sequence   FASTA