NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase

Tavolieri A, Murray D, Askenasy I, Pennington J, McGarry L, Stanley C, Stroupe M, Journal of Structural Biology 205(2):170-179 (2019) DOI

SASDKN7 – Sulfite reductase flavoprotein-60-ΔAAPSQS

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein)
MWexperimental 60 kDa
MWexpected 61 kDa
VPorod 73 nm3
log I(s) 2.63×10-1 2.63×10-2 2.63×10-3 2.63×10-4
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) small angle scattering data  s, nm-1
ln I(s)
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Guinier plot ln 2.64×10-1 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot 1.104 0 3 sRg
p(r)
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) pair distance distribution function Rg: 3.3 nm 0 Dmax: 11.3 nm

Data validation


Fits and models


log I(s)
 s, nm-1

SANS data from solutions of Sulfite reductase flavoprotein-60-ΔAAPSQS in 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH 7.8 were collected using the EQ-SANS (BL-6) beam line (Spallation Neutron Source, Oak Ridge National Laboratory, USA) equipped with a GE linear position-sensitive detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.25 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 8°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) (SiRFP-60)
Mol. type   Protein
Organism   Escherichia coli (strain K12)
Olig. state   Monomer
Mon. MW   60.7 kDa
 
UniProt   P38038 (53-599)
Sequence   FASTA