Crystal structure of a xylulose 5-phosphate phosphoketolase. insights into the substrate specificity for xylulose 5-phosphate.

Scheidig AJ, Horvath D, Szedlacsek SE, J Struct Biol (2019) Europe PMC

SASDEF5 – Phosphoketolase (L. lactis) with 1 mM thiaminpyrophosphate and 2% v/v glycerol at pH 7.0

Probable phosphoketolase
MWI(0) 146 kDa
MWexpected 191 kDa
VPorod 237 nm3
log I(s) 2.12×104 2.12×103 2.12×102 2.12×101
Probable phosphoketolase small angle scattering data  s, nm-1
ln I(s)
Probable phosphoketolase Guinier plot ln 2.13×104 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Probable phosphoketolase Kratky plot 1.104 0 √3 sRg
p(r)
Probable phosphoketolase pair distance distribution function Rg: 3.4 nm 0 Dmax: 10.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Probable phosphoketolase PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
Probable phosphoketolase SASREF model
Synchrotron SAXS data from solutions of phosphoketolase in 20mM potassium phosphate, 150mM NaCl, 0.007 %(w/v) β-octyl glucoside, 1mM DTT, 1mM MgCl2, 1mM thiaminpyrophosphate, 2 % v/v glycerol, pH 7 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 20°C. 29 successive 0.045 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Probable phosphoketolase
Mol. type   Protein
Organism   Lactococcus lactis subsp. lactis
Olig. state   Dimer
Mon. MW   95.7 kDa
 
UniProt   Q9CFH4
Sequence   FASTA
 
PDB ID   6GUA