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

SASDRS4 – Mycobacterium tuberculosis phosphoserine phosphatase (MtSerB2) dimer

Phosphoserine phosphatase SerB2
MWexperimental 88 kDa
MWexpected 87 kDa
VPorod 141 nm3
log I(s) 9.36×10-2 9.36×10-3 9.36×10-4 9.36×10-5
Phosphoserine phosphatase SerB2 small angle scattering data  s, nm-1
ln I(s)
Phosphoserine phosphatase SerB2 Guinier plot ln 9.37×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoserine phosphatase SerB2 Kratky plot 1.104 0 3 sRg
p(r)
Phosphoserine phosphatase SerB2 pair distance distribution function Rg: 3.3 nm 0 Dmax: 10.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mycobacterium tuberculosis phosphoserine phosphatase (MtSerB2) 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 13.6 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. 31 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 SerB2 (MtSerB2)
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Dimer
Mon. MW   43.4 kDa
 
UniProt   O53289 (1-409)
Sequence   FASTA