Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs.

Josts I, Nitsche J, Maric S, Mertens HD, Moulin M, Haertlein M, Prevost S, Svergun DI, Busch S, Forsyth VT, Tidow H, Structure 26(8):1072-1079.e4 (2018) Europe PMC

SASDDF5 – NBD-MsbA (+1mM ADP)

Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA
MWexperimental 30 kDa
MWexpected 27 kDa
VPorod 50 nm3
log I(s) 2.20×10-2 2.20×10-3 2.20×10-4 2.20×10-5
Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA small angle scattering data  s, nm-1
ln I(s)
Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA Guinier plot ln 2.20×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA Kratky plot 1.104 0 √3 sRg
p(r)
Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA pair distance distribution function Rg: 2.1 nm 0 Dmax: 7.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of NBD-MsbA (+1mM ADP) in 30 mM Tris, 150 mM NaCl, 0.5 mM TCEP, 1 mM ADP, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 18.00 mg/ml was measured at 20°C. 20 successive 0.050 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.

Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA (NBD-MsbA)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   27.3 kDa
 
UniProt   P60752
Sequence   FASTA