Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.

Korasick DA, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ, FEBS J 284(18):3029-3049 (2017) Europe PMC

SASDCY3 – Proline utilization A from Desulfovibrio vulgaris 4.5 mg/mL

Bifunctional protein PutA
MWexperimental 222 kDa
MWexpected 229 kDa
VPorod 294 nm3
log I(s) 2.31×103 2.31×102 2.31×101 2.31×100
Bifunctional protein PutA small angle scattering data  s, nm-1
ln I(s)
Bifunctional protein PutA Guinier plot ln 2.32×103 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
Bifunctional protein PutA Kratky plot 1.104 0 √3 sRg
p(r)
Bifunctional protein PutA pair distance distribution function Rg: 4.6 nm 0 Dmax: 16 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Proline utilization A from Desulfovibrio vulgaris in 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM EDTA, and 0.5 mM THP at pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a MAR 165 CCD detector (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 4.5 mg/ml was measured. The data were normalized to the intensity of the transmitted beam and radially averaged. The radially averaged scattering of the solvent-blank was subtracted. X-ray wavelength, unknown; Exposure time, unknown; Sample-To-Detector distance, unknown.

Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Bifunctional protein PutA (DvPutA)
Mol. type   Protein
Organism   Desulfovibrio vulgaris
Olig. state   Dimer
Mon. MW   114.5 kDa
 
UniProt   A0A0E0T6R2
Sequence   FASTA