Crystal structure and solution scattering of Geobacillus stearothermophilus S9 peptidase reveal structural adaptations for carboxypeptidase activity.

Chandravanshi K, Singh R, Bhange GN, Kumar A, Yadav P, Kumar A, Makde RD, FEBS Lett (2024) Europe PMC

SASDSY8 – S9C peptidase from Geobacillus stearothermophilus

Acylamino-acid-releasing enzyme (I277L, V491A)
MWexperimental 306 kDa
MWexpected 308 kDa
VPorod 424 nm3
log I(s) 2.28×101 2.28×100 2.28×10-1 2.28×10-2
Acylamino-acid-releasing enzyme (I277L, V491A) small angle scattering data  s, nm-1
ln I(s)
Acylamino-acid-releasing enzyme (I277L, V491A) Guinier plot ln 2.29×101 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
Acylamino-acid-releasing enzyme (I277L, V491A) Kratky plot 1.104 0 √3 sRg
p(r)
Acylamino-acid-releasing enzyme (I277L, V491A) pair distance distribution function Rg: 4.7 nm 0 Dmax: 13 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Acylamino-acid-releasing enzyme (I277L, V491A) GASBOR model
log I(s)
 s, nm-1
Acylamino-acid-releasing enzyme (I277L, V491A) GASBOR model
log I(s)
 s, nm-1
Acylamino-acid-releasing enzyme (I277L, V491A) GASBOR model
Synchrotron SAXS data from solutions of S9C peptidase from Geobacillus stearothermophilus in 10 mM Tris, 100 mM NaCl, pH 8 were collected on the BL-18 beam line at INDUS-2 (Indore, India) using a MAR 345 Image Plate detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

X-ray exposure time = UNKNOWN.

Acylamino-acid-releasing enzyme (I277L, V491A) (S9Cgs)
Mol. type   Protein
Organism   Geobacillus stearothermophilus
Olig. state   Tetramer
Mon. MW   77.1 kDa
 
UniProt   A0A150M835 (17-670)
Sequence   FASTA