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

SASDL25 – Bacillus subtilis complex of diadenylate cyclase (CdaA:cytoplasmic domain) and phosphoglucosamine mutase (GlmM)

Cyclic di-AMP synthase CdaA
Phosphoglucosamine mutase
MWexperimental 130 kDa
MWexpected 144 kDa
VPorod 250 nm3
log I(s) 4.73×10-1 4.73×10-2 4.73×10-3 4.73×10-4
Cyclic di-AMP synthase CdaA Phosphoglucosamine mutase small angle scattering data  s, nm-1
ln I(s)
Cyclic di-AMP synthase CdaA Phosphoglucosamine mutase Guinier plot ln 4.73×10-1 Rg: 4.5 nm 0 (4.5 nm)-2 s2
(sRg)2I(s)/I(0)
Cyclic di-AMP synthase CdaA Phosphoglucosamine mutase Kratky plot 1.104 0 3 sRg
p(r)
Cyclic di-AMP synthase CdaA Phosphoglucosamine mutase pair distance distribution function Rg: 4.5 nm 0 Dmax: 16.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the complex formed between the cytoplasmic domain of diadenylate cyclase and phosphoglucosamine mutase (GlmM) 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 10 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW403 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
 
Phosphoglucosamine mutase (GlmM)
Mol. type   Protein
Organism   Bacillus subtilis (strain 168)
Olig. state   Dimer
Mon. MW   50.3 kDa
 
UniProt   O34824 (1-448)
Sequence   FASTA