Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery.

Bogner AN, Ji J, Tanner JJ, Protein Eng Des Sel (2022) Europe PMC

SASDQ68 – Minimal proline dehydrogenase domain of proline utilization A (SmPutADeltaAlpha2) 3.4 mg/mL

Minimal proline dehydrogenase domain of proline utilization A (design #2)
MWexperimental 78 kDa
MWexpected 87 kDa
VPorod 108 nm3
log I(s) 8.10×101 8.10×100 8.10×10-1 8.10×10-2
Minimal proline dehydrogenase domain of proline utilization A (design #2) small angle scattering data  s, nm-1
ln I(s)
Minimal proline dehydrogenase domain of proline utilization A (design #2) Guinier plot ln 8.10×101 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Minimal proline dehydrogenase domain of proline utilization A (design #2) Kratky plot 1.104 0 3 sRg
p(r)
Minimal proline dehydrogenase domain of proline utilization A (design #2) pair distance distribution function Rg: 3 nm 0 Dmax: 9.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Minimal proline dehydrogenase domain of proline utilization A (design #2) OTHER model

Synchrotron SAXS data from solutions of minimal proline dehydrogenase domain of proline utilization A (SmPutADeltaAlpha2) in 25 mM HEPES pH 7.6, 150 mM NaCl, and 1mM TCEP, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS: Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1234 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.30 mg/ml was measured at 20°C. 30 successive 0.330 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.

Minimal proline dehydrogenase domain of proline utilization A (design #2) (SmPutADeltaAlpha2)
Mol. type   Protein
Organism   Sinorhizobium meliloti
Olig. state   Dimer
Mon. MW   43.7 kDa
 
UniProt   F7X6I3
Sequence   FASTA