Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation

Sarah Atkinson.

SASDR75 – ATP-dependent RNA helicase DDX3X (amino acids 50-580)

ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580)
MWexperimental 60 kDa
MWexpected 62 kDa
VPorod 102 nm3
log I(s) 1.38×10-2 1.38×10-3 1.38×10-4 1.38×10-5
ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) small angle scattering data  s, nm-1
ln I(s)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) Guinier plot ln 1.38×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) Kratky plot 1.104 0 3 sRg
p(r)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) pair distance distribution function Rg: 3.7 nm 0 Dmax: 12.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of ATP-dependent RNA helicase DDX3X (50-580) in 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH 8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.4 m and at a wavelength of λ = 0.103 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 50.00 μl sample at 10 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 5/150 column at 16°C. 44 successive 1 second frames were collected through the sample 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.

ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   62.1 kDa
 
UniProt   O00571 (50-580)
Sequence   FASTA