c-di-AMP hydrolysis by a novel type of phosphodiesterase promotes differentiation of multicellular bacteria

Latoscha A, Drexler D, Al-Bassam M, Kaever V, Findlay K, Witte G, Tschowri N, (2019) DOI

SASDH35 – Soluble cyclic di-AMP binding protein CpeA (vnz_28055), regulator of CpeB

Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein)
MWexperimental 46 kDa
MWexpected 38 kDa
VPorod 69 nm3
log I(s) 3.20×10-2 3.20×10-3 3.20×10-4 3.20×10-5
Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) small angle scattering data  s, nm-1
ln I(s)
Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) Guinier plot ln 3.20×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) Kratky plot 1.104 0 √3 sRg
p(r)
Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of CpeA in 200 mM NaCl, 30 mM sodium phosphate, 5% (v/v) glycerol, pH 6.5 were collected on the EMBL P12 beam line at PETRA III (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.60 mg/ml was measured at 20°C. 35 successive 0.100 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.

Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) (CpeA)
Mol. type   Protein
Organism   Streptomyces venezuelae
Olig. state   Dimer
Mon. MW   19.1 kDa
 
UniProt   F2R9B6 (6-161)
Sequence   FASTA