Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.

Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D, Arch Biochem Biophys 653:24-38 (2018) Europe PMC

SASDDV3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 8 mg/ml of Wild-type C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase, reductase component
MWexperimental 67 kDa
MWexpected 71 kDa
VPorod 95 nm3
log I(s) 2.83×102 2.83×101 2.83×100 2.83×10-1
p-hydroxyphenylacetate 3-hydroxylase, reductase component small angle scattering data  s, nm-1
ln I(s)
p-hydroxyphenylacetate 3-hydroxylase, reductase component Guinier plot ln 2.83×102 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot 1.104 0 √3 sRg
p(r)
p-hydroxyphenylacetate 3-hydroxylase, reductase component pair distance distribution function Rg: 2.5 nm 0 Dmax: 7.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of p-hydroxyphenylacetate 3-hydroxylase, reductase component: 8 mg/ml of Wild-type C1 in the absence of p-hydroxyphenylacetic acid (HPA) in 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, and 5% glycerol, pH 7 were collected on the BL1.3W beam line at the Synchrotron Light Research Institute (SLRI) storage ring (Nakhon Ratchasima, Thailand) using a Rayonix SX165 detector at a sample-detector distance of 1.3 m and at a wavelength of λ = 0.13776 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 16°C. One 600 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

p-hydroxyphenylacetate 3-hydroxylase, reductase component (C1 reductase)
Mol. type   Protein
Organism   Acinetobacter baumannii
Olig. state   Dimer
Mon. MW   35.4 kDa
 
UniProt   Q6Q271
Sequence   FASTA