Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization.

Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM, FEBS J (2019) Europe PMC

SASDEK8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode

farnesylated human Guanylate-binding protein 1
MWexperimental 64 kDa
MWexpected 69 kDa
VPorod 102 nm3
log I(s) 1.39×101 1.39×100 1.39×10-1 1.39×10-2
farnesylated human Guanylate-binding protein 1 small angle scattering data  s, nm-1
ln I(s)
farnesylated human Guanylate-binding protein 1 Guinier plot ln 1.39×101 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
farnesylated human Guanylate-binding protein 1 Kratky plot 1.104 0 √3 sRg
p(r)
farnesylated human Guanylate-binding protein 1 pair distance distribution function Rg: 4.0 nm 0 Dmax: 14.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
farnesylated human Guanylate-binding protein 1 PYMOL model
log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1) in 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH 7.9 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 = 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.30 mg/ml was measured at 22°C. 10 successive 3 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.

farnesylated human Guanylate-binding protein 1 (farn-hGBP1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   69.2 kDa
 
UniProt   P32455 (1-592)
Sequence   FASTA
 
PDB ID   1F5N