Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition

Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W, Nature Communications 13(1) (2022) DOI

SASDKK3 – SEC-SAXS of Presequence Protease (PreP)

Presequence protease, mitochondrial
MWexperimental 113 kDa
MWexpected 115 kDa
VPorod 170 nm3
log I(s) 3.96×10-2 3.96×10-3 3.96×10-4 3.96×10-5
Presequence protease, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Presequence protease, mitochondrial Guinier plot ln 3.97×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Presequence protease, mitochondrial Kratky plot 1.104 0 √3 sRg
p(r)
Presequence protease, mitochondrial pair distance distribution function Rg: 3.1 nm 0 Dmax: 9.1 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of SEC-SAXS of Presequence Protease (PreP) in 20 mM Tris, 100 mM NaCl, pH 7.7 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus 100K detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A sample was injected at a 1.40 ml/min flow rate onto a GE Superdex 200 10/300 column at 22°C. One 0.500 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Sample injection volume = UNKNOWN

Presequence protease, mitochondrial (PreP)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   114.8 kDa
 
UniProt   Q5JRX3 (33-1036)
Sequence   FASTA