Long-range structural defects by pathogenic mutations in most severe glucose-6-phosphate dehydrogenase deficiency

Horikoshi N, Hwang S, Gati C, Matsui T, Castillo-Orellana C, Raub A, Garcia A, Jabbarpour F, Batyuk A, Broweleit J, Xiang X, Chiang A, Broweleit R, Vöhringer-Martinez E, Mochly-Rosen D, Wakatsuki S, Proceedings of the National Academy of Sciences 118(4) (2021) DOI

SASDJ35 – Glucose-6-phosphate dehydrogenase dimer

Glucose-6-phosphate 1-dehydrogenase
MWexperimental 119 kDa
MWexpected 119 kDa
VPorod 160 nm3
log I(s) 1.45×10-2 1.45×10-3 1.45×10-4 1.45×10-5
Glucose-6-phosphate 1-dehydrogenase small angle scattering data  s, nm-1
ln I(s)
Glucose-6-phosphate 1-dehydrogenase Guinier plot ln 1.45×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Glucose-6-phosphate 1-dehydrogenase Kratky plot 1.104 0 √3 sRg
p(r)
Glucose-6-phosphate 1-dehydrogenase pair distance distribution function Rg: 3.7 nm 0 Dmax: 12.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Glucose-6-phosphate 1-dehydrogenase PYMOL model
Synchrotron SAXS data from solutions of Glucose-6-phosphate dehydrogenase dimer in 20 mM Tris, 150 mM NaCl, pH 8 were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSRL) storage ring (Menlo Park, CA, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 1.7 m and at a wavelength of λ = 0.112756 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.20 mg/ml was measured at 25°C. 164 successive 1 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.

Glucose-6-phosphate 1-dehydrogenase (G6PD)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   59.5 kDa
 
UniProt   P11413 (1-515)
Sequence   FASTA
 
PDB ID   2BL9