Structural basis for the inhibition of the Bacillus subtilis c-di-AMP cyclase CdaA by the phosphoglucomutase GlmM

Pathania M, Tosi T, Millership C, Hoshiga F, Morgan R, Freemont P, Gründling A, Journal of Biological Chemistry :101317 (2021) DOI

SASDLY4 – Bacillus subtilis diadenylate cyclase CdaA: cytoplasmic domain

Cyclic di-AMP synthase CdaA
MWexperimental 42 kDa
MWexpected 44 kDa
VPorod 60 nm3
log I(s) 2.58×10-3 2.58×10-4 2.58×10-5 2.58×10-6
Cyclic di-AMP synthase CdaA small angle scattering data  s, nm-1
ln I(s)
Cyclic di-AMP synthase CdaA Guinier plot ln 2.59×10-3 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Cyclic di-AMP synthase CdaA Kratky plot 1.104 0 3 sRg
p(r)
Cyclic di-AMP synthase CdaA pair distance distribution function Rg: 2.9 nm 0 Dmax: 8.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the cytoplasmic domain of diadenylate cyclase from Bacillus subtilis in 30 mM Tris, 150 mM NaCl, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 0.5 mg/ml was injected at a 0.07 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 15°C. 620 successive 3 second frames were collected through the entire elution profile. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the SEC-peak sample scattering frames.

Sample detector distance = UNKNOWN

Cyclic di-AMP synthase CdaA (Diadenylate cyclase)
Mol. type   Protein
Organism   Bacillus subtilis (strain 168)
Olig. state   Dimer
Mon. MW   22.0 kDa
 
UniProt   Q45589 (97-273)
Sequence   FASTA