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