A morpheein equilibrium regulates catalysis in phosphoserine phosphatase SerB2 from Mycobacterium tuberculosis.

Pierson E, De Pol F, Fillet M, Wouters J, Commun Biol 6(1):1024 (2023) Europe PMC

SASDRW4 – Mycobacterium avium phosphoserine phosphatase (MaSerB) dimer

Phosphoserine phosphatase (G31R, G152E)
MWexperimental 91 kDa
MWexpected 88 kDa
VPorod 138 nm3
log I(s) 1.09×10-1 1.09×10-2 1.09×10-3 1.09×10-4
Phosphoserine phosphatase (G31R, G152E) small angle scattering data  s, nm-1
ln I(s)
Phosphoserine phosphatase (G31R, G152E) Guinier plot ln 1.10×10-1 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoserine phosphatase (G31R, G152E) Kratky plot 1.104 0 3 sRg
p(r)
Phosphoserine phosphatase (G31R, G152E) pair distance distribution function Rg: 3.3 nm 0 Dmax: 10.1 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Phosphoserine phosphatase (G31R, G152E) DADIMODO model

Synchrotron SAXS data from solutions of Mycobacterium avium phosphoserine phosphatase (MaSerB) dimer in 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH 7.4 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 13 mg/ml was injected at a 0.50 ml/min flow rate onto a BioResolve SEC mAb 200Å 2.5 µm, 7.8 x 300 mm column at 10°C. 11 successive 1 second frames were collected through the sample elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Phosphoserine phosphatase (G31R, G152E) (MaSerB)
Mol. type   Protein
Organism   Mycobacterium avium (strain 104)
Olig. state   Dimer
Mon. MW   43.9 kDa
 
UniProt   A0QJI1 (2-411)
Sequence   FASTA