Conformational dynamics of the membrane-anchored foldase LipH from Pseudomonas aeruginosa facilitates recognition and release of the client lipase

Jens Reiners.

SASDYM9 – Lipase chaperone (LipH) VD

Lipase chaperone
MWexperimental 39 kDa
MWexpected 38 kDa
VPorod 70 nm3
log I(s) 2.52×10-2 2.52×10-3 2.52×10-4 2.52×10-5
Lipase chaperone small angle scattering data  s, nm-1
ln I(s)
Lipase chaperone Guinier plot ln 2.52×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Lipase chaperone Kratky plot 1.104 0 √3 sRg
p(r)
Lipase chaperone pair distance distribution function Rg: 3.4 nm 0 Dmax: 12.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Lipase chaperone (LipH) VD Rg histogram Rg, nm
Lipase chaperone EOM/RANCH model
Lipase chaperone EOM/RANCH model
Lipase chaperone EOM/RANCH model
Lipase chaperone EOM/RANCH model
SAXS data from solutions of Lipase chaperone (LipH) VD in 50 mM Tris, 100 mM NaCl, 100 µM TCEP, 5% glycerol,, pH 8 were collected on the Xenocs Xeuss 2.0 Q-Xoom instrument (Center for Structural Studies, Heinrich-Heine-University, Düsseldorf, Germany) using a Pilatus3 R 300K detector at a sample-detector distance of 0.6 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 11.82 mg/ml was measured at 10°C. 24 successive 600 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Lipase chaperone (LipH VD)
Mol. type   Protein
Organism   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Olig. state   Monomer
Mon. MW   38.3 kDa
 
UniProt   Q01725
Sequence   FASTA