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

SASDKN3 – SEC-SAXS of Presequence Protease (PreP) with Amyloid beta precursor protein (1-40)

Presequence protease, mitochondrial
Amyloid-beta precursor protein
MWexperimental 111 kDa
MWexpected 119 kDa
VPorod 175 nm3
log I(s) 2.00×10-2 2.00×10-3 2.00×10-4 2.00×10-5
Presequence protease, mitochondrial Amyloid-beta precursor protein small angle scattering data  s, nm-1
ln I(s)
Presequence protease, mitochondrial Amyloid-beta precursor protein Guinier plot ln 2×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Presequence protease, mitochondrial Amyloid-beta precursor protein Kratky plot 1.104 0 3 sRg
p(r)
Presequence protease, mitochondrial Amyloid-beta precursor protein pair distance distribution function Rg: 3.1 nm 0 Dmax: 8.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of SEC-SAXS of Presequence Protease (PreP) with Amyloid beta precursor protein (1-40) in 20 mM Tris, 100 mM NaCl , 20 mM EDTA, 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
 
Amyloid-beta precursor protein
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   4.3 kDa
 
UniProt   P05067 (688-711)
Sequence   FASTA