Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus.

Davies JS, Coombes D, Horne CR, Pearce FG, Friemann R, North RA, Dobson RCJ, FEBS Lett (2018) Europe PMC

SASDEB6 – Staphylococcus aureus glucosamine-6-phosphate deaminase

Glucosamine-6-phosphate deaminase
MWexperimental 56 kDa
MWexpected 57 kDa
VPorod 84 nm3
log I(s) 6.79×10-2 6.79×10-3 6.79×10-4 6.79×10-5
Glucosamine-6-phosphate deaminase small angle scattering data  s, nm-1
ln I(s)
Glucosamine-6-phosphate deaminase Guinier plot ln 6.79×10-2 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Glucosamine-6-phosphate deaminase Kratky plot 1.104 0 √3 sRg
p(r)
Glucosamine-6-phosphate deaminase pair distance distribution function Rg: 2.8 nm 0 Dmax: 8.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Glucosamine-6-phosphate deaminase PYMOL model
Synchrotron SAXS data from solutions of Staphylococcus aureus glucosamine-6-phosphate deaminase in 20 mM Tris-HCl, 150 mM NaCl, pH 8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Dectris Pilatus 1M detector at a sample-detector distance of 1.6 m and at a wavelength of λ = 0.10332 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.00 mg/ml was measured at 20°C. 999 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.

Glucosamine-6-phosphate deaminase
Mol. type   Protein
Organism   Staphylococcus aureus
Olig. state   Dimer
Mon. MW   28.5 kDa
 
UniProt   A8YZR7
Sequence   FASTA
 
PDB ID   1HOT