DacA, GlmM and the DacA/GlmM complex

Tommaso Tosi.

SASDE88 – Solution structure of phosphoglucosamine mutase (GlmM) from Staphylococcus aureus

Phosphoglucosamine mutase
MWexperimental 94 kDa
MWexpected 99 kDa
VPorod 134 nm3
log I(s) 1.13×10-1 1.13×10-2 1.13×10-3 1.13×10-4
Phosphoglucosamine mutase small angle scattering data  s, nm-1
ln I(s)
Phosphoglucosamine mutase Guinier plot ln 1.14×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoglucosamine mutase Kratky plot 1.104 0 3 sRg
p(r)
Phosphoglucosamine mutase pair distance distribution function Rg: 3.8 nm 0 Dmax: 12.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Phosphoglucosamine mutase DAMFILT model

Synchrotron SAXS data from solutions of the GlmM in 30 mM Tris, 150 mM NaCl, pH 7.5 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK) using a Pilatus 2M detector at a sample-to-detector distance of 4.014 m and X-ray wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20°C using the following parameters: Column: Superdex 200 5/150 (GE Healthcare); Flow rate: 0.075 mL/min; Sample injection concentration: 12.0 mg/mL; Injection volume: 45 μL. The data obtained through the sample elution peak (collected as consecutive 3 s exposures) were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.

Phosphoglucosamine mutase (GlmM)
Mol. type   Protein
Organism   Staphylococcus aureus (strain USA300)
Olig. state   Dimer
Mon. MW   49.7 kDa
 
UniProt   Q2FEX1
Sequence   FASTA