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

SASDEL8 – Human Guanylate Binding Protein 1 (hGBP1), batch mode

human Guanylate-binding protein 1
MWI(0) 100 kDa
MWexpected 69 kDa
VPorod 162 nm3
log I(s) 1.00×102 1.00×101 1.00×100 1.00×10-1
human Guanylate-binding protein 1 small angle scattering data  s, nm-1
ln I(s)
human Guanylate-binding protein 1 Guinier plot ln 1.00×102 Rg: 5.1 nm 0 (5.1 nm)-2 s2
(sRg)2I(s)/I(0)
human Guanylate-binding protein 1 Kratky plot 1.104 0 √3 sRg
p(r)
human Guanylate-binding protein 1 pair distance distribution function Rg: 5.5 nm 0 Dmax: 27.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
human Guanylate-binding protein 1 PYMOL model
log I(s)
 s, nm-1
human Guanylate-binding protein 1 PYMOL model
log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of Human Guanylate Binding Protein 1 (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 2.00 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.

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