Structural analysis and functional evaluation of the disordered ß–hexosyltransferase region from Hamamotoa (Sporobolomyces) singularis

Dagher S, Vaishnav A, Stanley C, Meilleur F, Edwards B, Bruno-Bárcena J, Frontiers in Bioengineering and Biotechnology 11 (2023) DOI

SASDN67 – beta-hexosyl transferase (23-594), 4 mg/mL

Beta-galactosidase-like enzyme
MWexperimental 150 kDa
MWexpected 129 kDa
VPorod 236 nm3
log I(s) 1.98×101 1.98×100 1.98×10-1 1.98×10-2
Beta-galactosidase-like enzyme small angle scattering data  s, nm-1
ln I(s)
Beta-galactosidase-like enzyme Guinier plot ln 1.98×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Beta-galactosidase-like enzyme Kratky plot 1.104 0 √3 sRg
p(r)
Beta-galactosidase-like enzyme pair distance distribution function Rg: 3.8 nm 0 Dmax: 12.5 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of beta-hexosyl transferase in 5 mM sodium phosphate, pH 5 were collected using a Rigaku BioSAXS-2000 instrument at the Oak Ridge National Laboratory (Oak Ridge, TN, USA) equipped with a Pilatus 100K detector at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 22°C. Eight successive 300 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Beta-galactosidase-like enzyme
Mol. type   Protein
Organism   Hamamotoa singularis
Olig. state   Dimer
Mon. MW   64.3 kDa
 
UniProt   Q564N5 (23-594)
Sequence   FASTA