Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts.

Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P, Mol Cell 62(1):47-62 (2016) Europe PMC

SASDB84 – CyaA Block V

Adenylate cyclase toxin Block V
MWI(0) 13 kDa
MWexpected 16 kDa
VPorod 24 nm3
log I(s) 2.26×103 2.26×102 2.26×101 2.26×100
Adenylate cyclase toxin Block V small angle scattering data  s, nm-1
ln I(s)
Adenylate cyclase toxin Block V Guinier plot ln 2.27×103 Rg: 1.8 nm 0 (1.8 nm)-2 s2
(sRg)2I(s)/I(0)
Adenylate cyclase toxin Block V Kratky plot 1.104 0 3 sRg
p(r)
Adenylate cyclase toxin Block V pair distance distribution function Rg: 1.8 nm 0 Dmax: 5.9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Adenylate cyclase toxin Block V DAMMIF model

Synchrotron SAXS data from solutions of CyaA Block V in 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH 8 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 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.

Adenylate cyclase toxin Block V (CyaA Block V)
Mol. type   Protein
Organism   Bordetella pertussis
Olig. state   Monomer
Mon. MW   16 kDa
 
UniProt   P0DKX7
Sequence   FASTA