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

SASDRV4 – Mycobacterium marinum phosphoserine phosphatase (MmSerB2) dimer

phosphoserine phosphatase
MWexperimental 91 kDa
MWexpected 88 kDa
VPorod 138 nm3
log I(s) 1.01×10-1 1.01×10-2 1.01×10-3 1.01×10-4
phosphoserine phosphatase small angle scattering data  s, nm-1
ln I(s)
phosphoserine phosphatase Guinier plot ln 1.02×10-1 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
phosphoserine phosphatase Kratky plot 1.104 0 3 sRg
p(r)
phosphoserine phosphatase pair distance distribution function Rg: 3.3 nm 0 Dmax: 9.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mycobacterium marinum phosphoserine phosphatase (MmSerB2) 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 12.8 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 (MmSerB2)
Mol. type   Protein
Organism   Mycobacterium marinum (strain ATCC BAA-535 / M)
Olig. state   Dimer
Mon. MW   43.8 kDa
 
UniProt   B2HHH0 (2-411)
Sequence   FASTA