Structural and Functional Investigation of Putative Peptidase from Mycolicibacterium phlei : An Exclusive Endopeptidase among S9C Subfamily

Chandravanshi K, Jamdar S, Singh R, Kumar A, Mahato A, Agrawal R, Kumar S, Kumar A, Makde R, Biochemistry (2025) DOI

SASDVH8 – S9 peptidase form Mycobacterium phlei (4 mg/ml)

Peptidase S9
MWexperimental 318 kDa
MWexpected 304 kDa
VPorod 563 nm3
log I(s) 7.64×100 7.64×10-1 7.64×10-2 7.64×10-3
Peptidase S9 small angle scattering data  s, nm-1
ln I(s)
Peptidase S9 Guinier plot ln 7.65×100 Rg: 5.1 nm 0 (5.1 nm)-2 s2
(sRg)2I(s)/I(0)
Peptidase S9 Kratky plot 1.104 0 √3 sRg
p(r)
Peptidase S9 pair distance distribution function Rg: 5.1 nm 0 Dmax: 16.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Peptidase S9 GASBOR model
log I(s)
 s, nm-1
Peptidase S9 GASBOR model
log I(s)
 s, nm-1
Peptidase S9 ALPHAFOLD model
Synchrotron SAXS data from solutions of S9 peptidase form Mycobacterium phlei 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 = 0.1033 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

Peptidase S9 (S9mp)
Mol. type   Protein
Organism   Mycolicibacterium phlei DSM 43239 = CCUG 21000
Olig. state   Tetramer
Mon. MW   75.9 kDa
 
UniProt   A0A5N5URA7 (4-661)
Sequence   FASTA