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

SASDCX3 – Proline utilization A from Desulfovibrio vulgaris 3.0 mg/mL

Bifunctional protein PutA

MW^experimental	224	kDa
MW^expected	229	kDa
V^Porod	295	nm³

log I(s) 1.60×10³ 1.60×10² 1.60×10¹ 1.60×10⁰

Bifunctional protein PutA small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 1.60×10³ R_g: 4.4 nm 0 (4.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 4.6 nm 0 D_max: 16 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.6

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.000
0.795

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from a solution 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. One solute concentration of 3 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

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

UniProt		A0A0E0T6R2
Sequence		FASTA