The domain architecture of protozoan protein J-DNA-binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity.

Adamopoulos A, Heidebrecht T, Roosendaal J, Touw WG, Phan IQ, Beijnen J, Perrakis A, J Biol Chem (2019) Europe PMC

SASDGQ2 – Thymine dioxygenase lacking the JDNA binding domain Delta-JDBD (Δ-JDBD)

Delta-JDBD
MWexperimental 76 kDa
MWexpected 72 kDa
VPorod 108 nm3
log I(s) 1.00×102 1.00×101 1.00×100 1.00×10-1
Delta-JDBD small angle scattering data  s, nm-1
ln I(s)
Delta-JDBD Guinier plot ln 1.01×102 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Delta-JDBD Kratky plot 1.104 0 3 sRg
p(r)
Delta-JDBD pair distance distribution function Rg: 3.1 nm 0 Dmax: 9.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of thymine dioxygenase lacking the J-DNA binding domain (Δ-JDBD) in 20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 40.00 μl sample at 10.3 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 4°C. 50 successive 1 second frames were collected through the SEC elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN

Delta-JDBD (Δ-JDBD)
Mol. type   Protein
Organism   Leismania tarentolae
Olig. state   Monomer
Mon. MW   72.5 kDa
 
UniProt   Q9U6M1 (2-827)
Sequence   FASTA