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