Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.

Werten S, Rustmeier NH, Gemmer M, Virolle MJ, Hinrichs W, FEBS Lett (2019) Europe PMC

SASDF76 – Polyphosphate-targeting protein A

Polyphosphate-targeting protein A
MWI(0) 59 kDa
MWexpected 79 kDa
VPorod 124 nm3
log I(s) 4.53×103 4.53×102 4.53×101 4.53×100
Polyphosphate-targeting protein A small angle scattering data  s, nm-1
ln I(s)
Polyphosphate-targeting protein A Guinier plot ln 4.53×103 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Polyphosphate-targeting protein A Kratky plot 1.104 0 3 sRg
p(r)
Polyphosphate-targeting protein A pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Polyphosphate-targeting protein A CORAL model

Synchrotron SAXS data from solutions of Polyphosphate-targeting protein A in 20 mM Tris-HCl 400 mM NaCl, pH 7.4 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 5.5 mg/ml were measured at 10°C. 20 successive 0.050 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Polyphosphate-targeting protein A (PptA)
Mol. type   Protein
Organism   Streptomyces chartreusis
Olig. state   Dimer
Mon. MW   39.6 kDa
 
UniProt   A0A2N9BBV4 (1-374)
Sequence   FASTA