Structural adaptations for carboxypeptidase activity in putative S9 acylaminoacyl peptidase from Bacillus subtilis.

Chandravanshi K, Singh R, Kumar A, Bhange GN, Kumar A, Makde RD, Int J Biol Macromol :136734 (2024) Europe PMC

SASDV75 – S9 carboxypeptidase from Bacillus subtilis (4 mg/ml)

Putative acylaminoacyl-peptidase
MWexperimental 304 kDa
MWexpected 293 kDa
VPorod 439 nm3
log I(s) 8.52×100 8.52×10-1 8.52×10-2 8.52×10-3
Putative acylaminoacyl-peptidase small angle scattering data  s, nm-1
ln I(s)
Putative acylaminoacyl-peptidase Guinier plot ln 8.52×100 Rg: 5.2 nm 0 (5.2 nm)-2 s2
(sRg)2I(s)/I(0)
Putative acylaminoacyl-peptidase Kratky plot 1.104 0 √3 sRg
p(r)
Putative acylaminoacyl-peptidase pair distance distribution function Rg: 5.0 nm 0 Dmax: 15.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Putative acylaminoacyl-peptidase GASBOR model
log I(s)
 s, nm-1
Putative acylaminoacyl-peptidase ALPHAFOLD model
Synchrotron SAXS data from solutions of S9 carboxypeptidase from Bacillus subtilis in 10 mM Tris-HCL, 135 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 4.00 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. Number of frames = UNKNOWN

Putative acylaminoacyl-peptidase
Mol. type   Protein
Organism   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)
Olig. state   Tetramer
Mon. MW   73.3 kDa
 
UniProt   E0U0N4 (2-657)
Sequence   FASTA