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

SASDEA6 – Staphylococcus aureus N-acetylglucosamine-6-phosphate deacetylase dimer

N-acetylglucosamine-6-phosphate deacetylase
MWexperimental 82 kDa
MWexpected 86 kDa
VPorod 107 nm3
log I(s) 5.49×10-2 5.49×10-3 5.49×10-4 5.49×10-5
N-acetylglucosamine-6-phosphate deacetylase small angle scattering data  s, nm-1
ln I(s)
N-acetylglucosamine-6-phosphate deacetylase Guinier plot ln 5.49×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
N-acetylglucosamine-6-phosphate deacetylase Kratky plot 1.104 0 √3 sRg
p(r)
N-acetylglucosamine-6-phosphate deacetylase pair distance distribution function Rg: 3.2 nm 0 Dmax: 10.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
N-acetylglucosamine-6-phosphate deacetylase PYMOL model
Synchrotron SAXS data from solutions of Staphylococcus aureus N-acetylglucosamine-6-phosphate deacetylase dimer 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 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.

N-acetylglucosamine-6-phosphate deacetylase (NagA)
Mol. type   Protein
Organism   Staphylococcus aureus
Olig. state   Dimer
Mon. MW   43.1 kDa
 
UniProt   A0A0H2XGG9
Sequence   FASTA
 
PDB ID   2VHL