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

SASDGR2 – Thymine dioxygenase J-containing DNA binding domain (JDBD)

J-DNA binding domain
MWexperimental 28 kDa
MWexpected 21 kDa
VPorod 38 nm3
log I(s) 7.14×100 7.14×10-1 7.14×10-2 7.14×10-3
J-DNA binding domain small angle scattering data  s, nm-1
ln I(s)
J-DNA binding domain Guinier plot ln 7.14×100 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
J-DNA binding domain Kratky plot 1.104 0 3 sRg
p(r)
J-DNA binding domain pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.1 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the thymine dioxygenase J-containing DNA binding domain (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 3.8 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 75 Increase 10/300 column at 4°C. 34 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

J-DNA binding domain (JDBD)
Mol. type   Protein
Organism   Leishmania tarentolae
Olig. state   Monomer
Mon. MW   21.2 kDa
 
UniProt   Q9U6M1 (382-561)
Sequence   FASTA