Structural analysis and functional study of phosphofructokinase B (PfkB) from Mycobacterium marinum

Gao B, Ji R, Li Z, Su X, Li H, Sun Y, Ji C, Gan J, Li J, Biochemical and Biophysical Research Communications (2021) DOI

SASDQ85 – Phosphofructokinase B (PfkB) from Mycobacterium marinum

Fructokinase, PfkB
MWexperimental 36 kDa
MWexpected 32 kDa
VPorod 58 nm3
log I(s) 1.64×101 1.64×100 1.64×10-1 1.64×10-2
Fructokinase, PfkB small angle scattering data  s, nm-1
ln I(s)
Fructokinase, PfkB Guinier plot ln 1.65×101 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Fructokinase, PfkB Kratky plot 1.104 0 √3 sRg
p(r)
Fructokinase, PfkB pair distance distribution function Rg: 2.1 nm 0 Dmax: 6.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Fructokinase, PfkB DAMMIF model
Synchrotron SAXS data from solutions of phosphofructokinase B (PfkB) from Mycobacterium marinum in 20 mM Tris-HCl, 100 mM NaCl, pH 7.5 were collected on the BL19U2 beam line at the Shanghai Synchrotron Radiation Facility (SSRF; Shanghai, China) using a Pilatus 1M detector at a sample-detector distance of 2.6 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). A solute concentrations of 1 mg/ml were measured at 10°C. 60 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.

Fructokinase, PfkB
Mol. type   Protein
Organism   Mycobacterium marinum (strain ATCC BAA-535 / M)
Olig. state   Monomer
Mon. MW   31.6 kDa
 
UniProt   B2HEF4 (1-303)
Sequence   FASTA