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

SASDRU4 – Mycobacterium tuberculosis phosphoserine phosphatase (MtSerB2) trimer formed in the presence of L-serine

Phosphoserine phosphatase SerB2
MWexperimental 131 kDa
MWexpected 130 kDa
VPorod 200 nm3
log I(s) 4.21×10-2 4.21×10-3 4.21×10-4 4.21×10-5
Phosphoserine phosphatase SerB2 small angle scattering data  s, nm-1
ln I(s)
Phosphoserine phosphatase SerB2 Guinier plot ln 4.22×10-2 Rg: 4.0 nm 0 (4.0 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: 4.0 nm 0 Dmax: 14.3 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mycobacterium tuberculosis phosphoserine phosphatase (MtSerB2) trimer in 50 mM Tris, 150 mM NaCl, 1 mM TCEP, 10 mM L-serine, 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 25.00 μl sample at 14.4 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. 15 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   Trimer
Mon. MW   43.4 kDa
 
UniProt   O53289 (1-409)
Sequence   FASTA