The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms

Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M, Journal of Molecular Biology :169394 (2025) DOI

SASDU99 – Apolipoprotein A-I dimer, C-terminally truncated

Apolipoprotein A-I
MWexperimental 36 kDa
MWexpected 43 kDa
VPorod 58 nm3
log I(s) 9.11×10-3 9.11×10-4 9.11×10-5 9.11×10-6
Apolipoprotein A-I small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein A-I Guinier plot ln 9.12×10-3 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Apolipoprotein A-I Kratky plot 1.104 0 √3 sRg
p(r)
Apolipoprotein A-I pair distance distribution function Rg: 4.5 nm 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Apolipoprotein A-I DAMMIF model
Synchrotron SAXS data from solutions of C-terminally truncated Apolipoprotein A-I in 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a wavelength of λ = 0.1078 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 50.00 μl sample at 5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 12 successive 1 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Apolipoprotein A-I (ApoA-I)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   21.6 kDa
 
UniProt   P02647 (25-208)
Sequence   FASTA