A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide.

Hagelueken G, Clarke BR, Huang H, Tuukkanen A, Danciu I, Svergun DI, Hussain R, Liu H, Whitfield C, Naismith JH, Nat Struct Mol Biol 22(1):50-56 (2015) Europe PMC

SASDAH6 – WbdD(1-459)

bifunctional kinase- methyltransferase WbdD
MWI(0) 52 kDa
MWexpected 59 kDa
VPorod 90 nm3
log I(s) 4.74×101 4.74×100 4.74×10-1 4.74×10-2
bifunctional kinase- methyltransferase WbdD small angle scattering data  s, nm-1
ln I(s)
bifunctional kinase- methyltransferase WbdD Guinier plot ln 4.74×101 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
bifunctional kinase- methyltransferase WbdD Kratky plot 1.104 0 √3 sRg
p(r)
bifunctional kinase- methyltransferase WbdD pair distance distribution function Rg: 3.2 nm 0 Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
bifunctional kinase- methyltransferase WbdD CORAL model
log I(s)
 s, nm-1
bifunctional kinase- methyltransferase WbdD DAMMIN model
Synchrotron SAXS data from solutions of WbdD(1-459) in 20 mM BisTris 50 mM NaCl 5 mM DTT, pH 7 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 10 mg/ml were measured at 20°C. 10 successive 15 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 low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Tags: X33
bifunctional kinase- methyltransferase WbdD (WbdD)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   59.2 kDa