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

SASDC34 – Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) R51E mutant 7.0 mg/mL

Proline dehydrogenase
MWexperimental 216 kDa
MWexpected 215 kDa
VPorod 289 nm3
log I(s) 3.55×102 3.55×101 3.55×100 3.55×10-1
Proline dehydrogenase small angle scattering data  s, nm-1
ln I(s)
Proline dehydrogenase Guinier plot ln 3.56×102 Rg: 4.5 nm 0 (4.5 nm)-2 s2
(sRg)2I(s)/I(0)
Proline dehydrogenase Kratky plot 1.104 0 √3 sRg
p(r)
Proline dehydrogenase pair distance distribution function Rg: 4.6 nm 0 Dmax: 14.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Proline dehydrogenase DAMMIF model
Proline dehydrogenase DAMFILT model
Synchrotron SAXS data from solutions of Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) R51E mutant in 50 mM Tris, 50 mM NaCl, 0.5 mM Tris(2-carboxyethyl)phosphine, and 5% (v/v) glycerol, pH 7.8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a a Pilatus3 X 2M detector. One solute concentration of 7 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.

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

Proline dehydrogenase (BjPutA R51E)
Mol. type   Protein
Organism   Bradyrhizobium diazoefficiens
Olig. state   Dimer
Mon. MW   107.5 kDa
 
UniProt   Q89E26
Sequence   FASTA