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

SASDCP3 – Proline utilization A from Bdellovibrio bacteriovorus

Bifunctional protein PutA

MW^experimental	225	kDa
MW^expected	219	kDa
V^Porod	287	nm³

log I(s) 1.13×10³ 1.13×10² 1.13×10¹ 1.13×10⁰

Bifunctional protein PutA small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 1.13×10³ R_g: 4.5 nm 0 (4.5 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: 14 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.5

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0
1.067

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of Proline utilization A from Bdellovibrio bacteriovorus in 50 mM Tris, 125 mM NaCl, 1 mM EDTA and 1 mM tris(3-hydroxypropyl)phosphine (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. 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. Concentration = UNKNOWN

Bifunctional protein PutA
Mol. type		Protein
Organism		Bdellovibrio bacteriovorus
Olig. state		Dimer
Mon. MW		109.5 kDa

UniProt		Q6MNK1
Sequence		FASTA