Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function.

Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ, J Biol Chem 291(46):24065-24075 (2016) Europe PMC

SASDDP2 – Sinorhizobium meliloti Proline Utilization A (PutA) at high concentration, 4.00 mg/ml

Sinorhizobium meliloti (SmPutA)
MWexperimental 196 kDa
MWexpected 132 kDa
VPorod 277 nm3
log I(s) 2.20×103 2.20×102 2.20×101 2.20×100
Sinorhizobium meliloti (SmPutA) small angle scattering data  s, nm-1
ln I(s)
Sinorhizobium meliloti (SmPutA) Guinier plot ln 2.21×103 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Sinorhizobium meliloti (SmPutA) Kratky plot 1.104 0 3 sRg
p(r)
Sinorhizobium meliloti (SmPutA) pair distance distribution function Rg: 3.9 nm 0 Dmax: 11.9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Sinorhizobium meliloti (SmPutA) MES-FOXS model
Sinorhizobium meliloti (SmPutA) MES-FOXS model

Synchrotron SAXS data from solutions of Sinorhizobium meliloti proline utilization A (PutA) in 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP and 50 mM NaCl, pH 7.8, were collected on the 12.3.1 SIBYLS beam line at the Advanced Light Source storage ring (ALS; Berkeley, CA, USA) using a MAR 165 CCD detector at a wavelength of λ = 0.1127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

The fit to the SAXS data is shown for a volume-fraction weighted mixture of monomers and dimers. The volume fraction of monomer and dimer are 0.48 and 0.52, respectively.

Sinorhizobium meliloti (SmPutA) (SmPutA)
Mol. type   Protein
Organism   Sinorhizobium meliloti
Olig. state   Monomer
Mon. MW   131.8 kDa
 
UniProt   F7X6I3
Sequence   FASTA