Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor.

Olson LJ, Misra SK, Ishihara M, Battaile KP, Grant OC, Sood A, Woods RJ, Kim JP, Tiemeyer M, Ren G, Sharp JS, Dahms NM, Commun Biol 3(1):498 (2020) Europe PMC

SASDHP4 – Palmitoyl-protein thioesterase 1 (PPT1)

Palmitoyl-protein thioesterase 1
MWI(0) 37 kDa
MWexpected 31 kDa
VPorod 54 nm3
log I(s) 4.72×100 4.72×10-1 4.72×10-2 4.72×10-3
Palmitoyl-protein thioesterase 1 small angle scattering data  s, nm-1
ln I(s)
Palmitoyl-protein thioesterase 1 Guinier plot ln 4.72×100 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
Palmitoyl-protein thioesterase 1 Kratky plot 1.104 0 √3 sRg
p(r)
Palmitoyl-protein thioesterase 1 pair distance distribution function Rg: 2.4 nm 0 Dmax: 9.8 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of palmitoyl-protein thioesterase 1 in 20 mM imidazole, 150 mM NaCl, 5 mM beta glycerol phosphate, 10 mM MnCl2, pH 6.4 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.5 m and at a wavelength of λ = 0.1 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 200.00 μl sample at 1 mg/ml was injected at a 0.75 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 22°C. 564 successive 0.500 second frames were collected through the entire SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the sample scattering SEC peak frames.

Palmitoyl-protein thioesterase 1 (PPT1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   31.3 kDa
 
UniProt   P50897 (28-306)
Sequence   FASTA