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

SASDGP2 – Thymine dioxygenase full length J-DNA binding protein (JBP1)

Thymine dioxygenase JBP1
MWexperimental 99 kDa
MWexpected 93 kDa
VPorod 128 nm3
log I(s) 2.81×101 2.81×100 2.81×10-1 2.81×10-2
Thymine dioxygenase JBP1 small angle scattering data  s, nm-1
ln I(s)
Thymine dioxygenase JBP1 Guinier plot ln 2.81×101 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Thymine dioxygenase JBP1 Kratky plot 1.104 0 3 sRg
p(r)
Thymine dioxygenase JBP1 pair distance distribution function Rg: 3.6 nm 0 Dmax: 12 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of thymine dioxygenase J-DNA binding protein (JBP1) 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 8.7 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 4°C. 35 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

Thymine dioxygenase JBP1 (JBP1)
Mol. type   Protein
Organism   Leishmania tarentolae
Olig. state   Monomer
Mon. MW   93.5 kDa
 
UniProt   Q9U6M1 (2-827)
Sequence   FASTA