Solution Structure of SpoIVB Reveals Mechanism of PDZ Domain-Regulated Protease Activity.

Xie X, Guo N, Xue G, Xie D, Yuan C, Harrison J, Li J, Jiang L, Huang M, Front Microbiol 10:1232 (2019) Europe PMC

SASDFJ3 – Maltose binding protein-SpoIVB peptidase fusion (MBP-SpoIVB)

SpoIVB peptidase (MBP fusion)
MWexperimental 78 kDa
MWexpected 80 kDa
VPorod 96 nm3
log I(s) 2.76×101 2.76×100 2.76×10-1 2.76×10-2
SpoIVB peptidase (MBP fusion) small angle scattering data  s, nm-1
ln I(s)
SpoIVB peptidase (MBP fusion) Guinier plot ln 2.76×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
SpoIVB peptidase (MBP fusion) Kratky plot 1.104 0 3 sRg
SpoIVB peptidase (MBP fusion) pair distance distribution function Rg: 4.0 nm 0 Dmax: 15.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
SpoIVB peptidase (MBP fusion) CHIMERA model

Synchrotron SAXS data from solutions of MBP-SpoIVB peptidase fusion protein in 20 mM Tris-HCl, 150 mM NaCl, 5% glycerol, pH 8 were collected on the BL19U2 beam line at the Shanghai Synchrotron Radiation Facility (SSRF, Shanghai, China) using a Pilatus 1M detector at a sample-detector distance of 2.3 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 10°C. 20 successive 1 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 originally deposited p(r) profile is included in the full entry zip archive.

SpoIVB peptidase (MBP fusion) (MBP-SpoIVB)
Mol. type   Protein
Organism   Bacillus subtilis
Olig. state   Monomer
Mon. MW   80.1 kDa
UniProt   P17896
Sequence   FASTA